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PMID:15918 | 2,3-diphosphoglycerate, nucleotide phosophate, and organic and inorganic phosphate levels during the early phases of diabetic ketoacidosis. | The relation between serum and red blood cell (RBC) inorganic phosphate levels, RBC 2,3-diphosphoglycerate (2,3-DPG) levels, RBC nucleotide phosphate (Pn), and RBC total phosphate (Pt) levels were studied during the early phases of treatment and recovery from diabetic ketoacidosis (DKA). A steady drop in serum inorganic phosphate was found during the first 24 hours of insulin treatment and was most profound at 24 hours. No statistically significant changes (P less than 0.05) were found in red cell inorganic phosphate or nucleotide phosphate levels during the 24-hour study period. The levels of total red cell phosphate were lower in this group of patients than in nonacidotic diabetic subjects and decreased slightly after 24 hours of treatment. The red cell 2,3-DPG levels were low at the initiation of therapy and remained low during the 24-hour study period. Glucose, bicarbonate, lactate, and ketone levels fell in linear patterns with treatment. In view of the current evidence for the effects of low 2,3-DPG on oxygen delivery and the relation of low serum phosphate levels to RBC glycolysis and 2,3-DPG formation, this study reemphasizes the need for phosphate replacement during the early phases of treatment of DKA. | 2,3-diphosphoglycerate, nucleotide phosophate, and organic and inorganic phosphate levels during the early phases of diabetic ketoacidosis. The relation between serum and red blood cell (RBC) inorganic phosphate levels, RBC 2,3-diphosphoglycerate (2,3-DPG) levels, RBC nucleotide phosphate (Pn), and RBC total phosphate (Pt) levels were studied during the early phases of treatment and recovery from diabetic ketoacidosis (DKA). A steady drop in serum inorganic phosphate was found during the first 24 hours of insulin treatment and was most profound at 24 hours. No statistically significant changes (P less than 0.05) were found in red cell inorganic phosphate or nucleotide phosphate levels during the 24-hour study period. The levels of total red cell phosphate were lower in this group of patients than in nonacidotic diabetic subjects and decreased slightly after 24 hours of treatment. The red cell 2,3-DPG levels were low at the initiation of therapy and remained low during the 24-hour study period. Glucose, bicarbonate, lactate, and ketone levels fell in linear patterns with treatment. In view of the current evidence for the effects of low 2,3-DPG on oxygen delivery and the relation of low serum phosphate levels to RBC glycolysis and 2,3-DPG formation, this study reemphasizes the need for phosphate replacement during the early phases of treatment of DKA. | [
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PMID:15920 | Stimulation of microsomal NADPH oxidation by quinone group-containing anticancer chemicals. | Several anticancer chemicals containing a quinone group were found to stimulate the aerobic oxidation of NADPH by liver microsomes. The enzyme responsible for the above reaction was identified as NADPH-cytochrome c reductase (EC 1.6.2.4), one of the microsomal flavoproteins. The fact that a catalytic amount (20 micronM) of these anticancer chemicals was sufficient to oxidize all the NADPH (100 micronM) indicates that they function as electron carries from the flavoprotein to molecular oxygen. As a corollary, Mitomycin-C and Carbazilquinone stimulated oxygen uptake by Ehrlich ascites tumor cells in the presence of glucose that Daunomycin and Adriamycin failed to do so, although the reason for it remains to be elucidated. Carbazilquinone, in contrast to others, also stimulated the microsomal NADH oxidation. | Stimulation of microsomal NADPH oxidation by quinone group-containing anticancer chemicals. Several anticancer chemicals containing a quinone group were found to stimulate the aerobic oxidation of NADPH by liver microsomes. The enzyme responsible for the above reaction was identified as NADPH-cytochrome c reductase (EC 1.6.2.4), one of the microsomal flavoproteins. The fact that a catalytic amount (20 micronM) of these anticancer chemicals was sufficient to oxidize all the NADPH (100 micronM) indicates that they function as electron carries from the flavoprotein to molecular oxygen. As a corollary, Mitomycin-C and Carbazilquinone stimulated oxygen uptake by Ehrlich ascites tumor cells in the presence of glucose that Daunomycin and Adriamycin failed to do so, although the reason for it remains to be elucidated. Carbazilquinone, in contrast to others, also stimulated the microsomal NADH oxidation. | [
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|
PMID:15921 | Late persistence of serum gamma-glutamyl transpeptidase activity after mononucleosis. Report of 3 cases. | gamma-Glutamyl transpeptidase (GGTP) is a sensitive but nonspecific index hepatobiliary disease. In infectious mononucleosis (IM) or the mononucleosis-like disease attributable to cytomegalovirus (cytomegalovirus-induced IM), GGTP reverted to normal later than aspartate aminotransferase and alkaline phosphatase. In three cases elevated serum GGTP activity persisted for up to 24 months -- raising the question of persistent 'post-IM' hepatitis. Such prolonged GGTP activity was unusual in other late IM specimens. Possible, but unlikely, causes for such persistent GGTP activity are an unusual degree of hepatic damage during acute IM, excessive induction of microsomal enzyme system activity by drugs, or unusual Epstein-Barr virus carrier state activation that might contribute to ongoing hepatic structural damage. Other markers of chronic hepatocellular disease including aspartate aminotrasferase, alkaline phosphatase, and bilirubin were normal in late specimens from these 3 patients. The cause of their persistent elevated GGTP activities remains unknown. | Late persistence of serum gamma-glutamyl transpeptidase activity after mononucleosis. Report of 3 cases. gamma-Glutamyl transpeptidase (GGTP) is a sensitive but nonspecific index hepatobiliary disease. In infectious mononucleosis (IM) or the mononucleosis-like disease attributable to cytomegalovirus (cytomegalovirus-induced IM), GGTP reverted to normal later than aspartate aminotransferase and alkaline phosphatase. In three cases elevated serum GGTP activity persisted for up to 24 months -- raising the question of persistent 'post-IM' hepatitis. Such prolonged GGTP activity was unusual in other late IM specimens. Possible, but unlikely, causes for such persistent GGTP activity are an unusual degree of hepatic damage during acute IM, excessive induction of microsomal enzyme system activity by drugs, or unusual Epstein-Barr virus carrier state activation that might contribute to ongoing hepatic structural damage. Other markers of chronic hepatocellular disease including aspartate aminotrasferase, alkaline phosphatase, and bilirubin were normal in late specimens from these 3 patients. The cause of their persistent elevated GGTP activities remains unknown. | [
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|
PMID:15922 | Medical management of Crohn's disease in adolescence. | The therapy of Crohn's disease in adolescence must balance the natural disease history of growth suppression, debilitation, and progression against possible drug-related adverse effects on growth and development. In contrast to published guidelines which usually suggest episodic and symptomatic treatment of relapses, we have attempted to suppress disease activity throughout adolescence. Sixteen consecutive adolescent patients treated with continuous medical therapy for a mean duration of 3.5 years are presented. Fourteen received long term prednisone therapy for maintenance of disease suppression. All 16 have been asymptomatic or have had only mild symptoms which did not interfere with regular activities. Only 1 subject had to be rehospitalized. He subsequently underwent bowel surgery. Aternate day corticosteroid administration has been attained in 11 patients; 10 are growing and developing at a normal rate. In total, 13 of 16 have achieved pubertal development appropriate for age. The 8 patients with distal ileal disease have had a consistently excellent response to medical therapy. There have been no major adverse effects from drug therapy. It is concluded that an effort to suppress disease activity continuously in adolsecents with Crohn's disease is warranted. Excellent symptomatic control and normal rate of growth can be expected in patients with primarily ileal disease. | Medical management of Crohn's disease in adolescence. The therapy of Crohn's disease in adolescence must balance the natural disease history of growth suppression, debilitation, and progression against possible drug-related adverse effects on growth and development. In contrast to published guidelines which usually suggest episodic and symptomatic treatment of relapses, we have attempted to suppress disease activity throughout adolescence. Sixteen consecutive adolescent patients treated with continuous medical therapy for a mean duration of 3.5 years are presented. Fourteen received long term prednisone therapy for maintenance of disease suppression. All 16 have been asymptomatic or have had only mild symptoms which did not interfere with regular activities. Only 1 subject had to be rehospitalized. He subsequently underwent bowel surgery. Aternate day corticosteroid administration has been attained in 11 patients; 10 are growing and developing at a normal rate. In total, 13 of 16 have achieved pubertal development appropriate for age. The 8 patients with distal ileal disease have had a consistently excellent response to medical therapy. There have been no major adverse effects from drug therapy. It is concluded that an effort to suppress disease activity continuously in adolsecents with Crohn's disease is warranted. Excellent symptomatic control and normal rate of growth can be expected in patients with primarily ileal disease. | [
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|
PMID:15919 | [Effect of the cell dose on the development of 2 transplantable tumors in a syngeneic host]. | The effects of different cell dose inoculation of plasmocitoma MOPC-315 and ADK-1t in Balb/c syngeneic mice are discussed in this work. Inoculated cell dose and neoplasia percent incidence have been noticed to be closely related, but unexpectedly two doses exist for each tumour, a comparatively small one and a definitely larger one, which cause nearly the same percent incidence. This paradox phenomenon is discussed also with reference to other researchers remarkers. | [Effect of the cell dose on the development of 2 transplantable tumors in a syngeneic host]. The effects of different cell dose inoculation of plasmocitoma MOPC-315 and ADK-1t in Balb/c syngeneic mice are discussed in this work. Inoculated cell dose and neoplasia percent incidence have been noticed to be closely related, but unexpectedly two doses exist for each tumour, a comparatively small one and a definitely larger one, which cause nearly the same percent incidence. This paradox phenomenon is discussed also with reference to other researchers remarkers. | [
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PMID:15923 | [Programmed breech deliveries (author's transl)]. | The question whether the termination of a breech pregnancy by a programmed breech delivery would reduce the fetal risk was investigated. In 71 of 433 singleton breech deliveries (16%) the breech delivery was induced by oxytocin infusion. There were 38 primigravidas and 33 multi-gravidas. The Apgar and pH values showed the same results as in 3904 vertex deliveries with spontaneous onset of labour. The duration of labour was shortened. The incidence of Caesarean Section in programmed breech deliveries was 9.86%. All 71 infants were mature and healthy. There were no perinatal deaths. The results show that the fetal risk in breech deliveries is reduced by programmed breech delivery to the same risk as in vertex deliveries with spontaneous onset of labour. | [Programmed breech deliveries (author's transl)]. The question whether the termination of a breech pregnancy by a programmed breech delivery would reduce the fetal risk was investigated. In 71 of 433 singleton breech deliveries (16%) the breech delivery was induced by oxytocin infusion. There were 38 primigravidas and 33 multi-gravidas. The Apgar and pH values showed the same results as in 3904 vertex deliveries with spontaneous onset of labour. The duration of labour was shortened. The incidence of Caesarean Section in programmed breech deliveries was 9.86%. All 71 infants were mature and healthy. There were no perinatal deaths. The results show that the fetal risk in breech deliveries is reduced by programmed breech delivery to the same risk as in vertex deliveries with spontaneous onset of labour. | [
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|
PMID:15931 | Relationship between undissociated acidity of gastric juice and gastric protein secreted in response to graded doses of pentagastrin in duodenal ulcer patients. | Concentrations of free and total hydrogen ions, total protein and pepsin were measured in gastric juice fractions collected during basal secretion and upon stimulation by graded doses of pentagastrin administered intravenously. Undissociated hydrogen ion and non-pepsin protein concentrations were calculated as derived quantities. The studies were carried out in nine patients with duodenal ulcer both before and after truncal vagotomy. It was found that after vagotomy the undissociated hydrogen ion concentration was significantly lower and non-pepsin protein higher than before the operation. No correlation was found between the two quantities both before and after vagotomy. It was concluded that in duodenal ulcer patients either not all non-pepsin protein takes part in buffering of hydrogen ions secreted by parietal cells, or that non-protein buffers play a more important role. | Relationship between undissociated acidity of gastric juice and gastric protein secreted in response to graded doses of pentagastrin in duodenal ulcer patients. Concentrations of free and total hydrogen ions, total protein and pepsin were measured in gastric juice fractions collected during basal secretion and upon stimulation by graded doses of pentagastrin administered intravenously. Undissociated hydrogen ion and non-pepsin protein concentrations were calculated as derived quantities. The studies were carried out in nine patients with duodenal ulcer both before and after truncal vagotomy. It was found that after vagotomy the undissociated hydrogen ion concentration was significantly lower and non-pepsin protein higher than before the operation. No correlation was found between the two quantities both before and after vagotomy. It was concluded that in duodenal ulcer patients either not all non-pepsin protein takes part in buffering of hydrogen ions secreted by parietal cells, or that non-protein buffers play a more important role. | [
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|
PMID:15935 | [Mycoses. Pathogenicity and diagnosis of dermatophytes, yeasts and molds]. | Human beings today living in high industrialized areas suffer more frequently from fungal diseases than before. This is due to the management in animal production, but also to the use of cosmetics and contraceptives, smoking cigarettes, wearing clothes of synthetic polymers and application of new drugs, like antibiotics, cytostatics, immunosuppressives and others, which favours the growth of certain fungi in and on the skin and inside the human body. Some mechanisms are known from the macroorganism which are able to protect man from fungal invasion. Effective in this way are the normal flora of the skin, gut and the mucous membranes, the enzymes digestive and the natural low pH of the healthy skin. The fungal growths are favoured when primary diseases of not-infectious genesis due to disorders in metabolism or endocrinium, vitamin deficiency, malabsorption, maldigestion, false and malnutrition, and diseases of the haemopoetic system exist. But also viral and bacterial infections stimulate the development of secondary fungal diseases. The pathogens belong to three groups, dermatophytes, yeasts and molds, which can be differentiated according to their behaviour in culture and in tissue. | [Mycoses. Pathogenicity and diagnosis of dermatophytes, yeasts and molds]. Human beings today living in high industrialized areas suffer more frequently from fungal diseases than before. This is due to the management in animal production, but also to the use of cosmetics and contraceptives, smoking cigarettes, wearing clothes of synthetic polymers and application of new drugs, like antibiotics, cytostatics, immunosuppressives and others, which favours the growth of certain fungi in and on the skin and inside the human body. Some mechanisms are known from the macroorganism which are able to protect man from fungal invasion. Effective in this way are the normal flora of the skin, gut and the mucous membranes, the enzymes digestive and the natural low pH of the healthy skin. The fungal growths are favoured when primary diseases of not-infectious genesis due to disorders in metabolism or endocrinium, vitamin deficiency, malabsorption, maldigestion, false and malnutrition, and diseases of the haemopoetic system exist. But also viral and bacterial infections stimulate the development of secondary fungal diseases. The pathogens belong to three groups, dermatophytes, yeasts and molds, which can be differentiated according to their behaviour in culture and in tissue. | [
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|
PMID:15936 | [Systemic immunologic diseases]. | The systemic manifestation of immunological diseases is due to the spread of antigen mostly bound to specific antibody. Vasculitis and serositis follow the deposition of immune complexes to membranes. Whereas heterologous antigen causes temporary immune reactions, autologous antigen induces chronically reactions with definite destruction of tissue. Therefore, immunosuppression is indicated in autoaggressive diseases with rapid progrediency. In temporary reactions, however, antiphlogistic drugs and corticosteroids are sufficient. | [Systemic immunologic diseases]. The systemic manifestation of immunological diseases is due to the spread of antigen mostly bound to specific antibody. Vasculitis and serositis follow the deposition of immune complexes to membranes. Whereas heterologous antigen causes temporary immune reactions, autologous antigen induces chronically reactions with definite destruction of tissue. Therefore, immunosuppression is indicated in autoaggressive diseases with rapid progrediency. In temporary reactions, however, antiphlogistic drugs and corticosteroids are sufficient. | [
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]
|
PMID:15937 | [Hormone producing gastrointestinal neoplasms]. | 1. Due to their common origin from the neural crest the hormonogenic cells of the intestinal tract show similar cyto-chemical and ultra-structural characteristics. 2. Hyperplasiae and tumors of these cells lead to excessive hormone production with its consequences on the reacting organs. 3. Hormone producing tumors can be confined to one organ only, but as multiple endocrine adenomatosis they can afflict several organs. 4. Diagnosis of most hormone producing tumors is possible with the adequate radio-immunologic tests. Radiologic and endoscopic examinations can contribute to the localization of the tumor. 5. Surgical resection of the tumor or of the reacting organs impaired by the overproduction of hormones from the tumor is the indicated therapy. Medicamentous therapy is rarely successful. 6. The growth of most hormonogenic tumors is relatively slow. Rates of survival of up to 30 years have been known, even after formation of metastases of the tumor. Effects of hormone overproduction on other organs can reduce the prognosis. | [Hormone producing gastrointestinal neoplasms]. 1. Due to their common origin from the neural crest the hormonogenic cells of the intestinal tract show similar cyto-chemical and ultra-structural characteristics. 2. Hyperplasiae and tumors of these cells lead to excessive hormone production with its consequences on the reacting organs. 3. Hormone producing tumors can be confined to one organ only, but as multiple endocrine adenomatosis they can afflict several organs. 4. Diagnosis of most hormone producing tumors is possible with the adequate radio-immunologic tests. Radiologic and endoscopic examinations can contribute to the localization of the tumor. 5. Surgical resection of the tumor or of the reacting organs impaired by the overproduction of hormones from the tumor is the indicated therapy. Medicamentous therapy is rarely successful. 6. The growth of most hormonogenic tumors is relatively slow. Rates of survival of up to 30 years have been known, even after formation of metastases of the tumor. Effects of hormone overproduction on other organs can reduce the prognosis. | [
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|
PMID:15939 | The differential diagnosis of crescentic glomerulonephritis. The pathology of specific lesions with prognostic implications. | Combined findings from light and electron microscopy with immunofluorescence studies make a definitive diagnosis possible in most cases of crescentic glomerulonephritis. The patient's prognosis and pattern of response to therapy are matters of immediate concern in the light of recent developments in nephrology. The frequency of crescentic lesions varies depending on the specific types of disease, but the idiopathic lesion is seldom seen. | The differential diagnosis of crescentic glomerulonephritis. The pathology of specific lesions with prognostic implications. Combined findings from light and electron microscopy with immunofluorescence studies make a definitive diagnosis possible in most cases of crescentic glomerulonephritis. The patient's prognosis and pattern of response to therapy are matters of immediate concern in the light of recent developments in nephrology. The frequency of crescentic lesions varies depending on the specific types of disease, but the idiopathic lesion is seldom seen. | [
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PMID:15940 | Three glucose 6-phosphate dehydrogenase variants found in Japan. | Three Japanese glucose 6-phosphate dehydrogenase (G6PD) variants were investigated. G6PD 'Mediterranean-like' had markedly decreased activity, normal electrophoretic mobility, low Km G6P, low Km NADP, increased utilization of all three substrate analogues (2-deoxy-G6P, Gal-6P, and deamino-NADP) and slightly decreased heat stability and slightly biphasic pH curve. G6PD 'Ogori' had markedly decreased activity, but otherwise normal characteristics. G6PD 'Hofu' had moderately decreased activity, normal electrophoretic mobility, slightly reduced Km G6P, normal Km NADP, normal utilization of 2-deoxy-G6P and Gal-6P, but increased utilization of deamino-NADP and normal heat stability as well as normal pH curve. | Three glucose 6-phosphate dehydrogenase variants found in Japan. Three Japanese glucose 6-phosphate dehydrogenase (G6PD) variants were investigated. G6PD 'Mediterranean-like' had markedly decreased activity, normal electrophoretic mobility, low Km G6P, low Km NADP, increased utilization of all three substrate analogues (2-deoxy-G6P, Gal-6P, and deamino-NADP) and slightly decreased heat stability and slightly biphasic pH curve. G6PD 'Ogori' had markedly decreased activity, but otherwise normal characteristics. G6PD 'Hofu' had moderately decreased activity, normal electrophoretic mobility, slightly reduced Km G6P, normal Km NADP, normal utilization of 2-deoxy-G6P and Gal-6P, but increased utilization of deamino-NADP and normal heat stability as well as normal pH curve. | [
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PMID:15941 | Tissue culture propagation of tropical foliage plants. | Procedures were established for clonal multiplication in vitro of Cordyline terminalis Kunth, Dracaena godseffiana Hort., Scindapsus aureus Engler, and Syngonium podophyllum Schott. Shoot tips of actively growing terminals were selected as explants for Cordyline and Dracaena, and lateral buds were employed for Scindapsus and Syngonium. The basal nutrient medium contained Murashige and Skoog salts, 3% sucrose, 100 mg per 1 i-inositol, and 0.4 mg per 1 thiamine-HCl. The optima with respect to auxin, cytokinin, adenine sulfate-2H2O, and NaH2PO4-H2O addenda were determined. Also assessed were the influences of certain physical qualities of the nutrient medium and of the light intensity of the culture environment. The multiplication of each of the four plants was achieved by repeatedly subculturing the shoots that arose in vitro. Rates of plant increase per year per explant were calculated conservatively to be as follows: Syngonium, 5,000:Scindapsus, 100,000; Dracena, 300,000; and Cordyline, 500,000. | Tissue culture propagation of tropical foliage plants. Procedures were established for clonal multiplication in vitro of Cordyline terminalis Kunth, Dracaena godseffiana Hort., Scindapsus aureus Engler, and Syngonium podophyllum Schott. Shoot tips of actively growing terminals were selected as explants for Cordyline and Dracaena, and lateral buds were employed for Scindapsus and Syngonium. The basal nutrient medium contained Murashige and Skoog salts, 3% sucrose, 100 mg per 1 i-inositol, and 0.4 mg per 1 thiamine-HCl. The optima with respect to auxin, cytokinin, adenine sulfate-2H2O, and NaH2PO4-H2O addenda were determined. Also assessed were the influences of certain physical qualities of the nutrient medium and of the light intensity of the culture environment. The multiplication of each of the four plants was achieved by repeatedly subculturing the shoots that arose in vitro. Rates of plant increase per year per explant were calculated conservatively to be as follows: Syngonium, 5,000:Scindapsus, 100,000; Dracena, 300,000; and Cordyline, 500,000. | [
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PMID:15942 | Early events in the induction of glutamine synthetase activity by hydrocortisone in embryonic chick neural retina. | Primary cultures of 10-day embryonic chick neural retinas were used to investigate early aspects of the mechanism of hydrocortisone action on glutamine synthetase activity. As little as 2 hr of hydrocortisone exposure served to initiate significant increases in the glutamine synthetase activity levels assayed after 24 hr culture. Time course studies indicated that the increase in glutamine synthetase activity observed after 24 hr in culture resulted from a two-phase rise in activity and that cycloheximide was effective in suppressing the second-phase rise. Additional inhibition studies demonstrated that the second-phase increase in enzyme activity required continuous protein synthesis during the initial 6 hr. The evidence suggests a mechanism of hydrocortisone action involving the production of a protein which is important for the induction of glutamine synthetase activity by hydrocortisone. | Early events in the induction of glutamine synthetase activity by hydrocortisone in embryonic chick neural retina. Primary cultures of 10-day embryonic chick neural retinas were used to investigate early aspects of the mechanism of hydrocortisone action on glutamine synthetase activity. As little as 2 hr of hydrocortisone exposure served to initiate significant increases in the glutamine synthetase activity levels assayed after 24 hr culture. Time course studies indicated that the increase in glutamine synthetase activity observed after 24 hr in culture resulted from a two-phase rise in activity and that cycloheximide was effective in suppressing the second-phase rise. Additional inhibition studies demonstrated that the second-phase increase in enzyme activity required continuous protein synthesis during the initial 6 hr. The evidence suggests a mechanism of hydrocortisone action involving the production of a protein which is important for the induction of glutamine synthetase activity by hydrocortisone. | [
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PMID:15945 | Production of protease and elastase by Pseudomonas aeruginosa strains isolated from patients. | Using 20 strains of Pseudomonas aeruginosa isolated from patients, production of protease, elastase, and collagenase was determined by shaking culture in either complex or semisynthetic medium. No collagenase was produced by any strain of P. aeruginosa. According to their production of protease and elastase in different media, the P. aeruginosa strains were divided into three groups: the first group can produce elastase in complex medium and both protease and elastase in semisynthetic medium; the second group cannot produce any proteolytic enzymes in complex medium but can produce any proteolytic enzymes in either medium; and the third group cannot produce any proteolytic enzymes in either medium. In spite of the differences in the ability of the strains to produce the enzymes, depending upon the origin of the strains, the protease or elastases produced in different broths were regarded as identical. | Production of protease and elastase by Pseudomonas aeruginosa strains isolated from patients. Using 20 strains of Pseudomonas aeruginosa isolated from patients, production of protease, elastase, and collagenase was determined by shaking culture in either complex or semisynthetic medium. No collagenase was produced by any strain of P. aeruginosa. According to their production of protease and elastase in different media, the P. aeruginosa strains were divided into three groups: the first group can produce elastase in complex medium and both protease and elastase in semisynthetic medium; the second group cannot produce any proteolytic enzymes in complex medium but can produce any proteolytic enzymes in either medium; and the third group cannot produce any proteolytic enzymes in either medium. In spite of the differences in the ability of the strains to produce the enzymes, depending upon the origin of the strains, the protease or elastases produced in different broths were regarded as identical. | [
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|
PMID:15946 | Antibacterial product of peritoneal exudate cell cultures from guinea pigs infected with mycobacteria, listeriae, and rickettsiae. | In an in vitro model of cellular immunity, the antibacterial product of immunologically mediated mononuclear cell activation was studied from guinea pigs infected with listeriae and rickettsiae and compared with the product previously described from animals infected with mycobacteria. We found that this product, active against gram-positive bacilli, appeared to be identical in the three different infections with regard to its heat stability, its chromatographic adsorption and elution pattern, its susceptibility to inactivation by proteolytic enzymes, and its antibacterial spectrum | Antibacterial product of peritoneal exudate cell cultures from guinea pigs infected with mycobacteria, listeriae, and rickettsiae. In an in vitro model of cellular immunity, the antibacterial product of immunologically mediated mononuclear cell activation was studied from guinea pigs infected with listeriae and rickettsiae and compared with the product previously described from animals infected with mycobacteria. We found that this product, active against gram-positive bacilli, appeared to be identical in the three different infections with regard to its heat stability, its chromatographic adsorption and elution pattern, its susceptibility to inactivation by proteolytic enzymes, and its antibacterial spectrum | [
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PMID:15947 | Nutrition and enterotoxin synthesis by enterotoxigenic strains of Escherichia coli: defined medium for production of heat-stable enterotoxin. | A defined medium has been developed which supports synthesis of heat-stable enterotoxin (ST) by porcine and bovine strains of enterotoxigenic (ENT+) Escherichia coli in levels equivalent or better than a complex Casamino Acids-salts medium. The medium components did not support production of heat-labile enterotoxin (LT) but were similar for ST synthesis by ENT+ strains producting only ST and those which produced ST in addition to LT. The amino acids in Casamino Acids found to be necessary for growth and enterotoxin synthesis were proline, serine, aspartic acid, and alanine. Maximal growth and toxin levels were obtained after 8 h of incubation. Improved growth, but not an increase in synthesis of ST, was observed in the presence of Mg2+, Mn2+ and Fe3+ compared with Mg2+ alone. A chelator, tricine, was necessary for maximal cell densities,, probably to solubilize trace ions and make them more available to the bacteria. Increased growth was observed upon addition of glucose to both complex and defined media; however, glucose as well as gluconate and pyruvate appeared to cause repression of toxin synthesis. Addition of vitamins, oleic acid, or DL-lactic acid to the defined medium slightly increased levels of ST. | Nutrition and enterotoxin synthesis by enterotoxigenic strains of Escherichia coli: defined medium for production of heat-stable enterotoxin. A defined medium has been developed which supports synthesis of heat-stable enterotoxin (ST) by porcine and bovine strains of enterotoxigenic (ENT+) Escherichia coli in levels equivalent or better than a complex Casamino Acids-salts medium. The medium components did not support production of heat-labile enterotoxin (LT) but were similar for ST synthesis by ENT+ strains producting only ST and those which produced ST in addition to LT. The amino acids in Casamino Acids found to be necessary for growth and enterotoxin synthesis were proline, serine, aspartic acid, and alanine. Maximal growth and toxin levels were obtained after 8 h of incubation. Improved growth, but not an increase in synthesis of ST, was observed in the presence of Mg2+, Mn2+ and Fe3+ compared with Mg2+ alone. A chelator, tricine, was necessary for maximal cell densities,, probably to solubilize trace ions and make them more available to the bacteria. Increased growth was observed upon addition of glucose to both complex and defined media; however, glucose as well as gluconate and pyruvate appeared to cause repression of toxin synthesis. Addition of vitamins, oleic acid, or DL-lactic acid to the defined medium slightly increased levels of ST. | [
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|
PMID:15948 | Osteomyelitis caused by mycobacterium fortuitum. | A case of osteomylitis of the foot and ankle bones with subsequent complications is presented. Antibiotic therapy was unsuccessful and a below-knee amputation was performed. A comparison of the various Mycobacteria species and their role as etiologic agents in osteomyelitis follows. | Osteomyelitis caused by mycobacterium fortuitum. A case of osteomylitis of the foot and ankle bones with subsequent complications is presented. Antibiotic therapy was unsuccessful and a below-knee amputation was performed. A comparison of the various Mycobacteria species and their role as etiologic agents in osteomyelitis follows. | [
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|
PMID:15949 | The effects of anesthetic drugs and disease on the chemical regulation of ventilation. | The anesthesiologist uses a wide spectrum of drugs, including inhalational general anesthetics, barbiturates, benzodiazepines, narcotics analgesics and their antagonists, and neuromuscular blocking drugs. All of these drugs in sufficient dose impair the ventilatory response to chemical stimuli, and may cause inadequate gas exchange. The effect of depression of ventilatory control depends on the magnitude of depression and the coexistence of functional abnormalities in the respiratory system. The functional abnormalities are the result of preexistent pulmonary disease or other disease processes that impair respiratory function, the anticipated effects of major surgery (e.g., pulmonary resection), and the complications of anesthesia and surgery. From a functional viewpoint, the mechanisms of the effects of these disease processes on ventilatory control are: (1) interference with the neurophysiological control of automatic ventilation; (2) impairment of peripheral or central chemoreceptor function; (3) impairment of respiratory muscle function; (4) increase in the mechanical load to breathing as a result of increased resistance or decreased compliance of the respiratory system; and (5) increase in the ventilatory requirements as a result of ventilation/blood flow maldistribution, metabolic acidosis, or increased metabolic rate. As a result of current trends in the use of multiple drugs and controlled ventilation during anesthesia, the patient is at greatest risk during the early postoperative period in the recovery room. In addition to the functional abnormalities described above, the probability of impaired gas exchange and respiratory failure is increased as a result of impaired metabolism and elimination of drugs as a result of hepatic and renal insufficiency, and acute changes in acidbase status, which alter the ionization and distribution of drugs. | The effects of anesthetic drugs and disease on the chemical regulation of ventilation. The anesthesiologist uses a wide spectrum of drugs, including inhalational general anesthetics, barbiturates, benzodiazepines, narcotics analgesics and their antagonists, and neuromuscular blocking drugs. All of these drugs in sufficient dose impair the ventilatory response to chemical stimuli, and may cause inadequate gas exchange. The effect of depression of ventilatory control depends on the magnitude of depression and the coexistence of functional abnormalities in the respiratory system. The functional abnormalities are the result of preexistent pulmonary disease or other disease processes that impair respiratory function, the anticipated effects of major surgery (e.g., pulmonary resection), and the complications of anesthesia and surgery. From a functional viewpoint, the mechanisms of the effects of these disease processes on ventilatory control are: (1) interference with the neurophysiological control of automatic ventilation; (2) impairment of peripheral or central chemoreceptor function; (3) impairment of respiratory muscle function; (4) increase in the mechanical load to breathing as a result of increased resistance or decreased compliance of the respiratory system; and (5) increase in the ventilatory requirements as a result of ventilation/blood flow maldistribution, metabolic acidosis, or increased metabolic rate. As a result of current trends in the use of multiple drugs and controlled ventilation during anesthesia, the patient is at greatest risk during the early postoperative period in the recovery room. In addition to the functional abnormalities described above, the probability of impaired gas exchange and respiratory failure is increased as a result of impaired metabolism and elimination of drugs as a result of hepatic and renal insufficiency, and acute changes in acidbase status, which alter the ionization and distribution of drugs. | [
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PMID:15951 | Biochemical and physiological approaches to opiate dependence. | Biochemical and physiological theories of opiate addiction are reviewed in an historical context. The biochemical evidence implicating acetylcholine and norepinephrine in the phenomena of tolerance and physical dependence is described, and the six major biochemical and physiological theories are reviewed, emphasizing their close ties (differing sometimes only linguistically) with late nineteenth century theories of tolerance and physical dependence. The operational-reductionistic approaches taken by these theorists, especially when defining psychic dependence, is criticized from a phenomenological point of view while also emphasizing that characteristics of the social structure and moral viewpoints must also be taken into account when studying these phenomena. | Biochemical and physiological approaches to opiate dependence. Biochemical and physiological theories of opiate addiction are reviewed in an historical context. The biochemical evidence implicating acetylcholine and norepinephrine in the phenomena of tolerance and physical dependence is described, and the six major biochemical and physiological theories are reviewed, emphasizing their close ties (differing sometimes only linguistically) with late nineteenth century theories of tolerance and physical dependence. The operational-reductionistic approaches taken by these theorists, especially when defining psychic dependence, is criticized from a phenomenological point of view while also emphasizing that characteristics of the social structure and moral viewpoints must also be taken into account when studying these phenomena. | [
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PMID:15952 | The activation of intravascular coagulation by bromocarbamide. | In the rabbit the application of a non-lethal, sleep-inducing dose of bromisovalerianyl carbamide (0.5 g/kg body weight) causes an activation of the coagulation system. This activation is manifested by shortened thrombin and partial thromboplastin times and a decrease of fibrinogen concentration and Factor V activity. In contrast, pentobarbital sodium at a dose (62.5 mg/kg) which causes the same changes in arterial partial oxygen pressure and arterial pH does not influence the coagulation system. The bromocarbamide-induced changes in the coagulation system are not to be considered as a result of hypoxia and acidosis but seem to be caused by early endothelial and tissue lesions which result in the release of procoagulatory substances. In healthy test persons a single dose of 1.5 g bromisovalerianyl carbamide has no demonstrable influence on the system of hemostasis. | The activation of intravascular coagulation by bromocarbamide. In the rabbit the application of a non-lethal, sleep-inducing dose of bromisovalerianyl carbamide (0.5 g/kg body weight) causes an activation of the coagulation system. This activation is manifested by shortened thrombin and partial thromboplastin times and a decrease of fibrinogen concentration and Factor V activity. In contrast, pentobarbital sodium at a dose (62.5 mg/kg) which causes the same changes in arterial partial oxygen pressure and arterial pH does not influence the coagulation system. The bromocarbamide-induced changes in the coagulation system are not to be considered as a result of hypoxia and acidosis but seem to be caused by early endothelial and tissue lesions which result in the release of procoagulatory substances. In healthy test persons a single dose of 1.5 g bromisovalerianyl carbamide has no demonstrable influence on the system of hemostasis. | [
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|
PMID:15955 | Hormonal control of zinc uptake and binding in the rat dorsolateral prostate. | The zinc uptake in the dorsolateral prostate of rats was studied after different hormonal manipulations. Orchiectomy reduced the uptake of 65Zn. Administration of estradiol benzoate to orchiectomized rats doubled the 65Zn uptake, a phenomenon which was not observed in orchiectomized-adrenalectomized rats. Adrenalectomy in orchiectomized rats had no effect on the concentration of radioactivity beyond the castration-induced decrease. A prolactin release inhibitor, 6-methyl-8-erogelenylacetamide, reduced the radioactivity concentration without changing the weight of the gland. Cyproterone acetate reduced the weight but not the radioactivity concentration. The concentration of 65Zn in the ventral prostate was not changed by orchiectomy, adrenalectomy, or the administration of estradiol benzoate, prolactin release inhibiors, or cyproterone acetate. The results suggest an important role for prolactin in the zinc uptake in the dorsolateral prostate but not in the ventral prostate. | Hormonal control of zinc uptake and binding in the rat dorsolateral prostate. The zinc uptake in the dorsolateral prostate of rats was studied after different hormonal manipulations. Orchiectomy reduced the uptake of 65Zn. Administration of estradiol benzoate to orchiectomized rats doubled the 65Zn uptake, a phenomenon which was not observed in orchiectomized-adrenalectomized rats. Adrenalectomy in orchiectomized rats had no effect on the concentration of radioactivity beyond the castration-induced decrease. A prolactin release inhibitor, 6-methyl-8-erogelenylacetamide, reduced the radioactivity concentration without changing the weight of the gland. Cyproterone acetate reduced the weight but not the radioactivity concentration. The concentration of 65Zn in the ventral prostate was not changed by orchiectomy, adrenalectomy, or the administration of estradiol benzoate, prolactin release inhibiors, or cyproterone acetate. The results suggest an important role for prolactin in the zinc uptake in the dorsolateral prostate but not in the ventral prostate. | [
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|
PMID:15956 | Plasma constituent (s) inhibiting platelet adhesiveness. | Adhesiveness in citrated whole blood is critically pH dependent at hydrogenion concentrations close to the physiological range. While platelets in platelet-rich plasma (PRP) adhere poorly in glass-bead columns, washed platelets and particularly gel-filtered platelets (GFP), prepared from PRP, are adhesive, Separation of PRP on a Sepharose 2B column revealed the presence of an inhibitor of adhesiveness of GFP. The inhibitory compound is thermostable and nondialyzable. It is inactivated completely by pronase digestion and partally by trypsin digestion. It is distinct from any one of the known platelet factors. Washed erythrocytes and erythrocyte membranes attenuate the potency of the inhibitor. Following separation by isoelectric focusing, the inhibitory activity is limited primarily to a single fraction with an isoelectric point of 5.1 containing equal amounts of proteins and lipids. Two protein bands are revealed by sodium dodecyl sulfate-gel electrophoresis of the purified fraction. It is concluded that PRP contains a compound, apparently a lipoprotein, which inhibits platelet adhesiveness. | Plasma constituent (s) inhibiting platelet adhesiveness. Adhesiveness in citrated whole blood is critically pH dependent at hydrogenion concentrations close to the physiological range. While platelets in platelet-rich plasma (PRP) adhere poorly in glass-bead columns, washed platelets and particularly gel-filtered platelets (GFP), prepared from PRP, are adhesive, Separation of PRP on a Sepharose 2B column revealed the presence of an inhibitor of adhesiveness of GFP. The inhibitory compound is thermostable and nondialyzable. It is inactivated completely by pronase digestion and partally by trypsin digestion. It is distinct from any one of the known platelet factors. Washed erythrocytes and erythrocyte membranes attenuate the potency of the inhibitor. Following separation by isoelectric focusing, the inhibitory activity is limited primarily to a single fraction with an isoelectric point of 5.1 containing equal amounts of proteins and lipids. Two protein bands are revealed by sodium dodecyl sulfate-gel electrophoresis of the purified fraction. It is concluded that PRP contains a compound, apparently a lipoprotein, which inhibits platelet adhesiveness. | [
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|
PMID:15957 | [Immunosuppressive agents for therapy of autoimmune diseases of the skin and of psoriasis]. | A review of immunosuppressive therapy of dermatoses is given. The pathogenesis of autoimmun diseases is discussed. The treatment of autoimmun diseases and of psoriasis with immunosuppressive drugs is ilucidated. | [Immunosuppressive agents for therapy of autoimmune diseases of the skin and of psoriasis]. A review of immunosuppressive therapy of dermatoses is given. The pathogenesis of autoimmun diseases is discussed. The treatment of autoimmun diseases and of psoriasis with immunosuppressive drugs is ilucidated. | [
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|
PMID:15960 | The hospitalized child with urticaria. | Patients with urticaria and angioedema admitted to CHMC were analyzed. The most common etiologic factor for the urticaria was infection (in 45% of the cases), while drugs or medications were responsible in 10% of patients. Almost half of the children received corticosteroids for the treatment of their urticaria. | The hospitalized child with urticaria. Patients with urticaria and angioedema admitted to CHMC were analyzed. The most common etiologic factor for the urticaria was infection (in 45% of the cases), while drugs or medications were responsible in 10% of patients. Almost half of the children received corticosteroids for the treatment of their urticaria. | [
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|
PMID:15974 | Formation and dissimilation of oxalacetate and pyruvate Pseudomonas citronellolis grown on noncarbohydrate substrates. | Metabolism of lactate as a carbon source by Pseudomonas citronellolis occurred via a nicotinamide adenine dinucleotide (NAD)-independent L-lactate dehydrogenase, which was present in cells grown on DL-lactate but was not present in cells grown on acetate, aspartate, citrate, glucose, glutamate, or malate. The cells also possessed a constitutive, NAD-independent malate dehydrogenase instead of the conventional NAD-dependent malate dehydrogenase instead of the conventional NAD-dependent enzyme in the tricarboxylic acid cycle. Both enzymes were particulate and used dichlorophenolindo-phenol or oxygen as an electron acceptor. In acetate-grown cells, the activity of pyruvate dehydrogenase and NAD phosphate-linked malate enzyme decreased, cells grown on glucose or lactate. This was consistent with the need to maintain a supply of oxalacetate for metabolism of acetate via the tricarboxylic acid cycle. Changes in enzyme activities suggest that gluconeogenesis from noncarbohydrate carbon sources occurs via the malate enzyme (when oxalacetate decarboxylase is inhibited) or a combination of the NAD-independent malate dehydrogenase and oxalacetate decarboxylase. | Formation and dissimilation of oxalacetate and pyruvate Pseudomonas citronellolis grown on noncarbohydrate substrates. Metabolism of lactate as a carbon source by Pseudomonas citronellolis occurred via a nicotinamide adenine dinucleotide (NAD)-independent L-lactate dehydrogenase, which was present in cells grown on DL-lactate but was not present in cells grown on acetate, aspartate, citrate, glucose, glutamate, or malate. The cells also possessed a constitutive, NAD-independent malate dehydrogenase instead of the conventional NAD-dependent malate dehydrogenase instead of the conventional NAD-dependent enzyme in the tricarboxylic acid cycle. Both enzymes were particulate and used dichlorophenolindo-phenol or oxygen as an electron acceptor. In acetate-grown cells, the activity of pyruvate dehydrogenase and NAD phosphate-linked malate enzyme decreased, cells grown on glucose or lactate. This was consistent with the need to maintain a supply of oxalacetate for metabolism of acetate via the tricarboxylic acid cycle. Changes in enzyme activities suggest that gluconeogenesis from noncarbohydrate carbon sources occurs via the malate enzyme (when oxalacetate decarboxylase is inhibited) or a combination of the NAD-independent malate dehydrogenase and oxalacetate decarboxylase. | [
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|
PMID:15975 | Cellulase of Neurospora crassa. | Mycelia and ungerminated conidia of Neurospora crassa were found to secrete extracellular endocellulase (EC 3.2.1.4). A simple induction system of potassium phosphate buffer (ph 6.0) plus inducer relied on the internal metabolic reserves of conicia or mycelia to provide energy and substrates for protein synthesis. Buffer concentration for optimum enzyme production was 100 mM, but at higher buffer concentrations enzyme production was inhibited. Cellobiose was clearly the best inducer, with an optimum effect from 0.05 to 1 mM. In deionized water, cellulase remained mostly associated with the cell, but a variety of salts stimulated the release of cellulase into the medium. | Cellulase of Neurospora crassa. Mycelia and ungerminated conidia of Neurospora crassa were found to secrete extracellular endocellulase (EC 3.2.1.4). A simple induction system of potassium phosphate buffer (ph 6.0) plus inducer relied on the internal metabolic reserves of conicia or mycelia to provide energy and substrates for protein synthesis. Buffer concentration for optimum enzyme production was 100 mM, but at higher buffer concentrations enzyme production was inhibited. Cellobiose was clearly the best inducer, with an optimum effect from 0.05 to 1 mM. In deionized water, cellulase remained mostly associated with the cell, but a variety of salts stimulated the release of cellulase into the medium. | [
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|
PMID:15976 | Phosphoribulokinase from Nitrobacter winogradskyi: activation by reduced nicotinamide adenine dinucleotide and inhibition by pyridoxal phosphate. | CO2 fixation by particle-free extracts from Nitrobacter winogradskyi increased by addition of reduced nicotinamide adenine dinucleotide (NADH). Ribulose-1,5-diphosphate, however, increased CO2 fixation, even in the absence of NADH. Phosphoribulokinase (EC 2.7.1.19) was the enzyme of Nitrobacter extracts that was activated specifically by NADH. Pyridoxal-5-phosphate inhibited both CO2 fixation and NADH-activated phosphoribulokinase from Nitrobacter. However, it did not affect phosphoribulokinase from spinach leaves. Since the spinach enzyme had also no requirement for reduced pyridine nucleotides, it appears that pyridoxal phosphate interferes only with the binding of NADH and not with the binding of ribulose-5-phosphate and adenosine-5'-triphosphate. The regulation of phosphoribulokinase activity by NADH provided Nitrobacter with an energy-dependent control mechanism of CO2 assimilation. | Phosphoribulokinase from Nitrobacter winogradskyi: activation by reduced nicotinamide adenine dinucleotide and inhibition by pyridoxal phosphate. CO2 fixation by particle-free extracts from Nitrobacter winogradskyi increased by addition of reduced nicotinamide adenine dinucleotide (NADH). Ribulose-1,5-diphosphate, however, increased CO2 fixation, even in the absence of NADH. Phosphoribulokinase (EC 2.7.1.19) was the enzyme of Nitrobacter extracts that was activated specifically by NADH. Pyridoxal-5-phosphate inhibited both CO2 fixation and NADH-activated phosphoribulokinase from Nitrobacter. However, it did not affect phosphoribulokinase from spinach leaves. Since the spinach enzyme had also no requirement for reduced pyridine nucleotides, it appears that pyridoxal phosphate interferes only with the binding of NADH and not with the binding of ribulose-5-phosphate and adenosine-5'-triphosphate. The regulation of phosphoribulokinase activity by NADH provided Nitrobacter with an energy-dependent control mechanism of CO2 assimilation. | [
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|
PMID:15977 | Extracellular phosphatases of Chlamydomonas reinhardi and their regulation. | Chlamydomonas reinhardi, cultured under normal growth conditions, secreted significant amounts of protein and carbohydrates but not lipids or nucleic acids. A fivefold increase in light intensity led to a tenfold increase in secreted protein and carbohydrate. Among the proteins secreted was acid phosphatase with a pH optimum at 4.8 like the enzyme in the cells. Phosphorus depleted algae grown on minimal orthophosphate contained and secreted both acid and alkaline phosphatase. The pH optimum of the intracellular alkaline phosphatase was 9.2. When phosphorus-depleted cells were grown with increasing orthophosphate, intra- and extracellular alkaline phosphatase was almost completely repressed and intra- and extracellular acid phosphatase was partially repressed. Extracellular acid and alkaline phosphatase increased with the age of the culture. Electrophoresis indicated only one acid and one alkaline phosphatase in phosphorus-satisfied and phosphorus-depleted cells. Chlamydomonas cells suspended in an inorganic salt solution secreted only acid phosphatase; the absence of any extr-cellular cytoplasmic marker enzyme indicated that there was little, if any, autolysis to account for the extracellular acid enzyme. Phosphorus-depleted cells were able to grow on organic phosphates as the sole source of orthophosphate. Ribose-5-phosphate was the best for cell multiplication, and its utility was shown to be due to the cell's ability to use the ribose as well as the orthophosphatase for cell multiplication. | Extracellular phosphatases of Chlamydomonas reinhardi and their regulation. Chlamydomonas reinhardi, cultured under normal growth conditions, secreted significant amounts of protein and carbohydrates but not lipids or nucleic acids. A fivefold increase in light intensity led to a tenfold increase in secreted protein and carbohydrate. Among the proteins secreted was acid phosphatase with a pH optimum at 4.8 like the enzyme in the cells. Phosphorus depleted algae grown on minimal orthophosphate contained and secreted both acid and alkaline phosphatase. The pH optimum of the intracellular alkaline phosphatase was 9.2. When phosphorus-depleted cells were grown with increasing orthophosphate, intra- and extracellular alkaline phosphatase was almost completely repressed and intra- and extracellular acid phosphatase was partially repressed. Extracellular acid and alkaline phosphatase increased with the age of the culture. Electrophoresis indicated only one acid and one alkaline phosphatase in phosphorus-satisfied and phosphorus-depleted cells. Chlamydomonas cells suspended in an inorganic salt solution secreted only acid phosphatase; the absence of any extr-cellular cytoplasmic marker enzyme indicated that there was little, if any, autolysis to account for the extracellular acid enzyme. Phosphorus-depleted cells were able to grow on organic phosphates as the sole source of orthophosphate. Ribose-5-phosphate was the best for cell multiplication, and its utility was shown to be due to the cell's ability to use the ribose as well as the orthophosphatase for cell multiplication. | [
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|
PMID:15978 | Alkaline phosphatase of Blastocladiella emersonii: partial purification and characterization. | Alkaline phosphomonoesterase (EC 3.1.3.1) activity from Blastocladiella emersonii, while displaying typically broad substrate specificity for phosphorylated organic compounds, exhibited nearly complete substrate preference for N-acetylglucosamine-6-phosphate over N-acetylglucosamine-1-phosphate. Enzyme in zoospore extracts was purified 43-fold by differential centrifugation followed by gel filtration (Sephadex G-200) and then by ion-exchange chromatography (diethylaminoethyl-cellulose). The partially purified enzyme displayed an apparent molecular weight (Sephadex G-200) of approximately 170,000. The activity of partially purified enzyme exhibited a pH optimum of pH 8.5, did not require a metal divalent cation, but was inhibitable by ethylenediaminetetraacetic acid. During the life cycle of the organism, the specific activity of the phosphatase decreased slightly during germination and early exponential growth but then increased about 4.5-fold during sporulation. B. emersonii alkaline phosphatase does not appear to be a repressible enzyme. | Alkaline phosphatase of Blastocladiella emersonii: partial purification and characterization. Alkaline phosphomonoesterase (EC 3.1.3.1) activity from Blastocladiella emersonii, while displaying typically broad substrate specificity for phosphorylated organic compounds, exhibited nearly complete substrate preference for N-acetylglucosamine-6-phosphate over N-acetylglucosamine-1-phosphate. Enzyme in zoospore extracts was purified 43-fold by differential centrifugation followed by gel filtration (Sephadex G-200) and then by ion-exchange chromatography (diethylaminoethyl-cellulose). The partially purified enzyme displayed an apparent molecular weight (Sephadex G-200) of approximately 170,000. The activity of partially purified enzyme exhibited a pH optimum of pH 8.5, did not require a metal divalent cation, but was inhibitable by ethylenediaminetetraacetic acid. During the life cycle of the organism, the specific activity of the phosphatase decreased slightly during germination and early exponential growth but then increased about 4.5-fold during sporulation. B. emersonii alkaline phosphatase does not appear to be a repressible enzyme. | [
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|
PMID:15979 | Effects of carbon dioxide, urea, and ammonia on growth of Ureaplasma urealyticum (T-strain mycoplasma). | By use of a simple device for continuous CO2 gassing of Ureaplasma urealyticum cultures growing in a liquid medium, we have been able to separate some of the effects of urea, CO2, ammonia, and pH on growth. The CO2 acted as a superior buffer in the pH range 5.7 to 6.8, which is optimal for Ureaplasma growth. It was, therefore, possible to observe the effect of repeated additions of urea to the culture without alkalinization of the growth medium. We found that the repeated additions of urea did not enhance Ureaplasma growth, and the resultant accumulation of ammonium ions (greater than 2,000 microng/ml) did not cause more rapid death under these conditions. By abruptly changing the gaseous environment from CO2 to N2, it was possible to cause a rapid pH change in the culture to a value above 8.0. This resulted in a more rapid death of the organisms. | Effects of carbon dioxide, urea, and ammonia on growth of Ureaplasma urealyticum (T-strain mycoplasma). By use of a simple device for continuous CO2 gassing of Ureaplasma urealyticum cultures growing in a liquid medium, we have been able to separate some of the effects of urea, CO2, ammonia, and pH on growth. The CO2 acted as a superior buffer in the pH range 5.7 to 6.8, which is optimal for Ureaplasma growth. It was, therefore, possible to observe the effect of repeated additions of urea to the culture without alkalinization of the growth medium. We found that the repeated additions of urea did not enhance Ureaplasma growth, and the resultant accumulation of ammonium ions (greater than 2,000 microng/ml) did not cause more rapid death under these conditions. By abruptly changing the gaseous environment from CO2 to N2, it was possible to cause a rapid pH change in the culture to a value above 8.0. This resulted in a more rapid death of the organisms. | [
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|
PMID:15980 | Localization of enzymes in Ureaplasma urealyticum (T-strain mycoplasma). | Ureaplasma urealyticum cells were lysed by osmotic shock or by digitonin. The membrane fraction contained four to ten times as much protein as the cytoplasmic fraction. These values are in large excess of those reported for classical mycoplasmas, suggesting that the Ureaplasma membrane fraction was heavily contaminated with proteins derived from the growth medium. The U. urealyticum urease activity was localized in the cytoplasmic fraction, whereas the adenosine triphosphatase activity was localized in the membrane fraction. Significant urease activity could be detected also in nonviable cells. Urea, at concentrations above 0.25 M, was mycoplasmastatic to Acholeplasma laidlawii, Mycoplasma hominis, and U. urealyticum, so that the Ureaplasma urease did not afford preferential protection against urea toxicity. The intracellular localization of the urease would be expected to release ammonia from urea in the cytoplasm. The ammonia will take up protons to become ammonium ions. It can be hypothesized that the intracellular NH4+ plays a role in proton elimination or acid-base balance, which might be coupled to an energy producing ion gradient and/or transport mechanisms. | Localization of enzymes in Ureaplasma urealyticum (T-strain mycoplasma). Ureaplasma urealyticum cells were lysed by osmotic shock or by digitonin. The membrane fraction contained four to ten times as much protein as the cytoplasmic fraction. These values are in large excess of those reported for classical mycoplasmas, suggesting that the Ureaplasma membrane fraction was heavily contaminated with proteins derived from the growth medium. The U. urealyticum urease activity was localized in the cytoplasmic fraction, whereas the adenosine triphosphatase activity was localized in the membrane fraction. Significant urease activity could be detected also in nonviable cells. Urea, at concentrations above 0.25 M, was mycoplasmastatic to Acholeplasma laidlawii, Mycoplasma hominis, and U. urealyticum, so that the Ureaplasma urease did not afford preferential protection against urea toxicity. The intracellular localization of the urease would be expected to release ammonia from urea in the cytoplasm. The ammonia will take up protons to become ammonium ions. It can be hypothesized that the intracellular NH4+ plays a role in proton elimination or acid-base balance, which might be coupled to an energy producing ion gradient and/or transport mechanisms. | [
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|
PMID:15981 | Cell envelope protection of alkaline phosphatase against acid denaturation in Escherichia coli. | The effects of a highly acidic environment on the cell-associated alkaline phosphatase activities of a smooth and a rough strain of Escherichia coli O8 have been examined. The observation that cell-associated enzyme is denatured to a lesser degree than purified enzyme suggests that the association of the enzyme with the cell envelope affords it some degree of protection from potentially disruptive agents in the environment. The degree of protection afforded the enzyme from pH denaturation appears to be dependent upon the presence of a complete lipopolysaccharide in the outer membrane of these strains. An abbreviation of the chemical structure of this cell envelope component produces a change in the outer membrane, resulting in increased susceptibility of the cells to a battery of antibiotics and to lysozyme and in a small, but significant, change in the sensitivity of the cell envelope-associated alkaline phosphatase to the denaturing effect of an acidic environment. | Cell envelope protection of alkaline phosphatase against acid denaturation in Escherichia coli. The effects of a highly acidic environment on the cell-associated alkaline phosphatase activities of a smooth and a rough strain of Escherichia coli O8 have been examined. The observation that cell-associated enzyme is denatured to a lesser degree than purified enzyme suggests that the association of the enzyme with the cell envelope affords it some degree of protection from potentially disruptive agents in the environment. The degree of protection afforded the enzyme from pH denaturation appears to be dependent upon the presence of a complete lipopolysaccharide in the outer membrane of these strains. An abbreviation of the chemical structure of this cell envelope component produces a change in the outer membrane, resulting in increased susceptibility of the cells to a battery of antibiotics and to lysozyme and in a small, but significant, change in the sensitivity of the cell envelope-associated alkaline phosphatase to the denaturing effect of an acidic environment. | [
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|
PMID:15982 | Properties of two phosphatases and a cyclic phosphodiesterase of Salmonella typhimurium. | The properties of three phosphatases from Salmonella typhimurium have been examined. A cyclic 2',3'-nucleotide phosphodiesterase (EC 3.1.4.d) hydrolyzes cyclic 2',3'-purine and -pyrimidine nucleotides, as well as 3'-mononucleotides, and has a pH optimum of about 7.5. It requires divalent cations for activity and has a molecular weight of 67,000. Acid hexose phosphatase (EC 3.1.2.2) possesses activity towards hexose phosphates as well as other sugar phosphates. The enzyme is apparently a dimer of 37,000-dalton subunits. Nonspecific acid phosphatase (EC 3.1.3.2) hydrolyzes a variety of phosphate esters, including nucleotides and sugar phosphates. The enzyme also hydrolyzes the phosphoric anhydride bonds of pyrophosphate and nucleotides. Michaelis constants of the nonspecific acid phosphatase for several of its substrates are in the 1 to 2 mM range. Nonspecific acid phosphatase is a dimer of 27,000-dalton subunits. | Properties of two phosphatases and a cyclic phosphodiesterase of Salmonella typhimurium. The properties of three phosphatases from Salmonella typhimurium have been examined. A cyclic 2',3'-nucleotide phosphodiesterase (EC 3.1.4.d) hydrolyzes cyclic 2',3'-purine and -pyrimidine nucleotides, as well as 3'-mononucleotides, and has a pH optimum of about 7.5. It requires divalent cations for activity and has a molecular weight of 67,000. Acid hexose phosphatase (EC 3.1.2.2) possesses activity towards hexose phosphates as well as other sugar phosphates. The enzyme is apparently a dimer of 37,000-dalton subunits. Nonspecific acid phosphatase (EC 3.1.3.2) hydrolyzes a variety of phosphate esters, including nucleotides and sugar phosphates. The enzyme also hydrolyzes the phosphoric anhydride bonds of pyrophosphate and nucleotides. Michaelis constants of the nonspecific acid phosphatase for several of its substrates are in the 1 to 2 mM range. Nonspecific acid phosphatase is a dimer of 27,000-dalton subunits. | [
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|
PMID:15983 | Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases. | Two new mutations are described which, together, eliminate essentially all the aminotransferase activity required for de novo biosynthesis of tyrosine, phenylalanine, and aspartic acid in a K-12 strain of Escherichia coli. One mutation, designated tyrB, lies at about 80 min on the E. coli map and inactivates the "tyrosine-repressible" tyrosine/phenylalanine aminotransferase. The second mutation, aspC, maps at about 20 min and inactivates a nonrespressible aspartate aminotransferase that also has activity on the aromatic amino acids. In ilvE- strains, which lack the branched-chain amino acid aminotransferase, the presence of either the tyrosine-repressible aminotransferase or the aspartate aminotransferase is sufficient for growth in the absence of exogenous tyrosine, phenylalanine, or aspartate; the tyrosine-repressible enzyme is also active in leucine biosynthesis. The ilvE gene product alone can reverse a phenylalanine requirement. Biochemical studies on extracts of strains carrying combinations of these aminotransferase mutations confirm the existence of two distinct enzymes with overlapping specificities for the alpha-keto acid analogues of tyrosine, phenylalanine, and aspartate. These enzymes can be distinguished by electrophoretic mobilities, by kinetic parameters using various substrates, and by a difference in tyrosine repressibility. In extracts of an ilvE- tyrB- aspC- triple mutant, no aminotransferase activity for the alpha-keto acids of tyrosine, phenylalanine, or aspartate could be detected. | Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases. Two new mutations are described which, together, eliminate essentially all the aminotransferase activity required for de novo biosynthesis of tyrosine, phenylalanine, and aspartic acid in a K-12 strain of Escherichia coli. One mutation, designated tyrB, lies at about 80 min on the E. coli map and inactivates the "tyrosine-repressible" tyrosine/phenylalanine aminotransferase. The second mutation, aspC, maps at about 20 min and inactivates a nonrespressible aspartate aminotransferase that also has activity on the aromatic amino acids. In ilvE- strains, which lack the branched-chain amino acid aminotransferase, the presence of either the tyrosine-repressible aminotransferase or the aspartate aminotransferase is sufficient for growth in the absence of exogenous tyrosine, phenylalanine, or aspartate; the tyrosine-repressible enzyme is also active in leucine biosynthesis. The ilvE gene product alone can reverse a phenylalanine requirement. Biochemical studies on extracts of strains carrying combinations of these aminotransferase mutations confirm the existence of two distinct enzymes with overlapping specificities for the alpha-keto acid analogues of tyrosine, phenylalanine, and aspartate. These enzymes can be distinguished by electrophoretic mobilities, by kinetic parameters using various substrates, and by a difference in tyrosine repressibility. In extracts of an ilvE- tyrB- aspC- triple mutant, no aminotransferase activity for the alpha-keto acids of tyrosine, phenylalanine, or aspartate could be detected. | [
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PMID:15984 | Energy-dependent incorporation of sphingolipid precursors and fatty acids in Bacteriodes melaninogenicus. | Washed cells of Bacteroides melaninogenicus are unable to incorporate the sphingolipid precursor 3-ketodihydrosphingosine (3KDS) or dihydrosphingosine into the complete sphingolipids ceramide phosphorylethanolamine (CPE) and ceramide phosphorylglycerol (CPG), whereas growing cultures are able to do so. This result suggested that an energy source was required by washed cells to initiate the incorporation of 3KDS. Investigation of a number of energy sources for B. melaninogenicus showed that glutamine was active in driving the incorporation of 3KDS. This system shows saturation kinetics. Besides glutamine, only asparagine and reduced nicotinamide adenine dinucleotide (NADH) are effective; glutamate and other compounds are inactive. The glutamine-driven system is sensitive to 2,4-dinitrophenol, azide, N,N'- dicyclohexylcarbodiimide, and carbonyl cyanide m-chlorophenylhydrazone. Asparagine plus NADH shows a synergistic effect in stimulating the incorporation of 3KDS into CPE and CPG in washed cells. However, glutamine plus NADH and glutamine plus asparagine show no such synergy. The cytochrome-free mutant of B. melaninogenicus, strain S, incorporates 3KDS in a manner similar to the parent strain when glutamine is used to drive the reaction; NADH or asparagine, however, are ineffective when used with strain S. Vitamin K-depleted cells of B. melaninogenicus are similar to vitamin K-grown cells, when glutamine or NADH is used to drive the 3KDS incorporation. Glutamine and NADH are also effective in stimulating the incorporation of palmitate and acetate by washed cells of B, melaninogenicus. Increased incorporation of these fatty acids into CPE, CPG, 3KDS, and other phospholipids is significantly increased by the presence of glutamine or NADH. Thus, energization of the membrane of B. melaninogenicus by glutamine or the electron transport system by NADH or asparagine is required for sphingolipid and other phospholipid synthesis. The relationship of this energization to possible transport of sphingolipid precursors is discussed. | Energy-dependent incorporation of sphingolipid precursors and fatty acids in Bacteriodes melaninogenicus. Washed cells of Bacteroides melaninogenicus are unable to incorporate the sphingolipid precursor 3-ketodihydrosphingosine (3KDS) or dihydrosphingosine into the complete sphingolipids ceramide phosphorylethanolamine (CPE) and ceramide phosphorylglycerol (CPG), whereas growing cultures are able to do so. This result suggested that an energy source was required by washed cells to initiate the incorporation of 3KDS. Investigation of a number of energy sources for B. melaninogenicus showed that glutamine was active in driving the incorporation of 3KDS. This system shows saturation kinetics. Besides glutamine, only asparagine and reduced nicotinamide adenine dinucleotide (NADH) are effective; glutamate and other compounds are inactive. The glutamine-driven system is sensitive to 2,4-dinitrophenol, azide, N,N'- dicyclohexylcarbodiimide, and carbonyl cyanide m-chlorophenylhydrazone. Asparagine plus NADH shows a synergistic effect in stimulating the incorporation of 3KDS into CPE and CPG in washed cells. However, glutamine plus NADH and glutamine plus asparagine show no such synergy. The cytochrome-free mutant of B. melaninogenicus, strain S, incorporates 3KDS in a manner similar to the parent strain when glutamine is used to drive the reaction; NADH or asparagine, however, are ineffective when used with strain S. Vitamin K-depleted cells of B. melaninogenicus are similar to vitamin K-grown cells, when glutamine or NADH is used to drive the 3KDS incorporation. Glutamine and NADH are also effective in stimulating the incorporation of palmitate and acetate by washed cells of B, melaninogenicus. Increased incorporation of these fatty acids into CPE, CPG, 3KDS, and other phospholipids is significantly increased by the presence of glutamine or NADH. Thus, energization of the membrane of B. melaninogenicus by glutamine or the electron transport system by NADH or asparagine is required for sphingolipid and other phospholipid synthesis. The relationship of this energization to possible transport of sphingolipid precursors is discussed. | [
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PMID:15985 | Regulation of galactose oxidase synthesis and secretion in Dactylium dendroides: effects of pH and culture density. | The effects of pH and growth density on the amount of an extracellular enzyme, galactose oxidase, synthesized by the fungus Dactylium dendroides were studied. Growth at a pH below 6.7 caused a decrease in the ability of the organism to release galactose oxidase. The enzyme retained by these fungal cells was liberated whenever the pH was raised to 7.0. Cycloheximide addition failed to inhibit the appearance of this protein; [3H]leucine added prior to pH adjustment was not incorporated into the released protein, These observations indicate the released protein is not newly synthesized protein. The retained enzyme would be secreted slowly over a 2-day period if the pH was not increased. In addition to regulating protein retention, pH was also shown to be associated with vacuolization, cell volume, culture density, and inhibition of protein synthesis. Cultures maintained at low pH were characterized by a dense growth consisting of highly vacuolated, buoyant, fungal hyphae. Increasing the pH from 6 to 7 caused a decrease in vacuole size. Cells grown at neutral pH maintained a lower density of growth and, based on activity measurements, synthesized 33% more galactose oxidase. Furthermore, cultures grown at pH 6.0 and maintained at a lower cell density produced galactose oxidase at a level similar to that of cells grown at neutral pH. Thus, the elevated density of the cell culture was inhibitory to galactose oxidase synthesis. The observed effects on protein synthesis and release were rather specific for galactose oxidase, since other extracellular proteins appeared in the earliest stages of growth. | Regulation of galactose oxidase synthesis and secretion in Dactylium dendroides: effects of pH and culture density. The effects of pH and growth density on the amount of an extracellular enzyme, galactose oxidase, synthesized by the fungus Dactylium dendroides were studied. Growth at a pH below 6.7 caused a decrease in the ability of the organism to release galactose oxidase. The enzyme retained by these fungal cells was liberated whenever the pH was raised to 7.0. Cycloheximide addition failed to inhibit the appearance of this protein; [3H]leucine added prior to pH adjustment was not incorporated into the released protein, These observations indicate the released protein is not newly synthesized protein. The retained enzyme would be secreted slowly over a 2-day period if the pH was not increased. In addition to regulating protein retention, pH was also shown to be associated with vacuolization, cell volume, culture density, and inhibition of protein synthesis. Cultures maintained at low pH were characterized by a dense growth consisting of highly vacuolated, buoyant, fungal hyphae. Increasing the pH from 6 to 7 caused a decrease in vacuole size. Cells grown at neutral pH maintained a lower density of growth and, based on activity measurements, synthesized 33% more galactose oxidase. Furthermore, cultures grown at pH 6.0 and maintained at a lower cell density produced galactose oxidase at a level similar to that of cells grown at neutral pH. Thus, the elevated density of the cell culture was inhibitory to galactose oxidase synthesis. The observed effects on protein synthesis and release were rather specific for galactose oxidase, since other extracellular proteins appeared in the earliest stages of growth. | [
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PMID:15986 | Morphology of Ureaplasma urealyticum (T-mycoplasma) organisms and colonies. | The morphology of Ureaplasm urealyticum in broth cultures was studied by phase-contrast microscopy. Most organisms appeared singly or in pairs. Long filaments and long chains of cocci, common in classical mycoplasma cultures, were not observed. On solid medium, U. urealyticum produced "fried-egg" colonies which developed according to the scheme suggested by Razin and Oliver (J. Gen. Microbiol., 1961) for the morphogenesis of the classical mycoplasma colonies. The formation of the peripheral zone of the colonies followed that of the central zone only when growth conditions were adequate, Hence, the appearance of peripheral zones, and consequently the larger colony size, can be taken as an indicator of improved growth conditions. Incubation in an atmosphere of 100% CO2 resulted in significantly larger colonies than in an atmosphere of N2, O2, or air. CO2 acts as a buffer, keeping the pH at the optimal range for Ureaplasma growth (pH 6.0 to 6.5) in the presence of the ammonia produced from the urea hydrolyzed by the organisms. The addition to the medium of 0.01 M urea together with 0.01 M putrescine enabled better growth than with urea alone. Small amounts of phosphate improved growth in an atmosphere of CO2, apparently fulfilling a nutritional role. Under nitrogen, higher phosphate concentrations were required for good growth, apparently serving as a buffer as well as a nutrient. Sodium chloride and sucrose which had been added to increase the tonicity of the medium inhibited growth above 0.1 M. An increase in the agar concentration above 2% resulted in decreased colony size. Likewise, prolonged drying of the agar plates caused a marked decrease in colony size, mostly affecting the peripheral zone. The addition of both urea and putrescine to the growth medium and incubation in a humidified CO2 atmosphere are recommended for improved growth and formation of fried-egg colonies of U. ureaplyticum on agar. It must be emphasized that these experiments were carried out with a laboratory-adapted strain. | Morphology of Ureaplasma urealyticum (T-mycoplasma) organisms and colonies. The morphology of Ureaplasm urealyticum in broth cultures was studied by phase-contrast microscopy. Most organisms appeared singly or in pairs. Long filaments and long chains of cocci, common in classical mycoplasma cultures, were not observed. On solid medium, U. urealyticum produced "fried-egg" colonies which developed according to the scheme suggested by Razin and Oliver (J. Gen. Microbiol., 1961) for the morphogenesis of the classical mycoplasma colonies. The formation of the peripheral zone of the colonies followed that of the central zone only when growth conditions were adequate, Hence, the appearance of peripheral zones, and consequently the larger colony size, can be taken as an indicator of improved growth conditions. Incubation in an atmosphere of 100% CO2 resulted in significantly larger colonies than in an atmosphere of N2, O2, or air. CO2 acts as a buffer, keeping the pH at the optimal range for Ureaplasma growth (pH 6.0 to 6.5) in the presence of the ammonia produced from the urea hydrolyzed by the organisms. The addition to the medium of 0.01 M urea together with 0.01 M putrescine enabled better growth than with urea alone. Small amounts of phosphate improved growth in an atmosphere of CO2, apparently fulfilling a nutritional role. Under nitrogen, higher phosphate concentrations were required for good growth, apparently serving as a buffer as well as a nutrient. Sodium chloride and sucrose which had been added to increase the tonicity of the medium inhibited growth above 0.1 M. An increase in the agar concentration above 2% resulted in decreased colony size. Likewise, prolonged drying of the agar plates caused a marked decrease in colony size, mostly affecting the peripheral zone. The addition of both urea and putrescine to the growth medium and incubation in a humidified CO2 atmosphere are recommended for improved growth and formation of fried-egg colonies of U. ureaplyticum on agar. It must be emphasized that these experiments were carried out with a laboratory-adapted strain. | [
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|
PMID:15987 | Extracellular acid protease of Aspergillus oryzae grown on liquid media: multiple forms due to association with heterogeneous polysaccharides. | The acid protease (EC 2.4.23.6) that is produced extracellularly when Aspergillus oryzae is grown on liquid media has been isolated and characterized. The enzyme was purified by precipitation with tannic acid, chromatography on Duolite A-2, and gel filtration on Sephadex G-100. The last step yielded four active components, with varying molecular weights ranging from 42,000 to 60,000. Two of them, designated E1 and E1a, with molecular weights of 60,000 and 55,000, respectively, were heterogeneous on isoelectric focusing, both giving at least three enzyme species with different isoelectric points, whereas the other two, E1b and E2, with molecular weights of 49,000 and 42,000, respectively, were essentially homogeneous. These four enzymes activated bovine pancreatic trypsinogen and had the same pH optima in the acid pH range. They had essentially the same amino acid composition and immunologically cross-reacted with each other. These catalytic, chemical, and immunological properties are similar to those of acid protease A1 and A2 from A. oryzae grown on solid bran media. Unlike acid protease from solid bran culture, which contains both carbohydrate-containing and the carbohydrate-free species, all of the four enzymes, E1, E1a, E1b, and E2, contained carbohydrate, ranging from 18.9 to 43% and comprising three hexoses, glucose, galactose, and mannose. The carbohydrate portions were polysaccharide in nature and heterogeneous with respect to both molecular weight and sugar composition, and at least a part of the carbohydrate was present in the form of homopolysaccharides such as galactan and mannan. These findings indicate that polysaccharide chains with different molecular weights and with different chemical compositions are apparently responsible for the microheterogeneity of acid protease. | Extracellular acid protease of Aspergillus oryzae grown on liquid media: multiple forms due to association with heterogeneous polysaccharides. The acid protease (EC 2.4.23.6) that is produced extracellularly when Aspergillus oryzae is grown on liquid media has been isolated and characterized. The enzyme was purified by precipitation with tannic acid, chromatography on Duolite A-2, and gel filtration on Sephadex G-100. The last step yielded four active components, with varying molecular weights ranging from 42,000 to 60,000. Two of them, designated E1 and E1a, with molecular weights of 60,000 and 55,000, respectively, were heterogeneous on isoelectric focusing, both giving at least three enzyme species with different isoelectric points, whereas the other two, E1b and E2, with molecular weights of 49,000 and 42,000, respectively, were essentially homogeneous. These four enzymes activated bovine pancreatic trypsinogen and had the same pH optima in the acid pH range. They had essentially the same amino acid composition and immunologically cross-reacted with each other. These catalytic, chemical, and immunological properties are similar to those of acid protease A1 and A2 from A. oryzae grown on solid bran media. Unlike acid protease from solid bran culture, which contains both carbohydrate-containing and the carbohydrate-free species, all of the four enzymes, E1, E1a, E1b, and E2, contained carbohydrate, ranging from 18.9 to 43% and comprising three hexoses, glucose, galactose, and mannose. The carbohydrate portions were polysaccharide in nature and heterogeneous with respect to both molecular weight and sugar composition, and at least a part of the carbohydrate was present in the form of homopolysaccharides such as galactan and mannan. These findings indicate that polysaccharide chains with different molecular weights and with different chemical compositions are apparently responsible for the microheterogeneity of acid protease. | [
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|
PMID:15988 | Choline metabolism in pneumococci. | Phosphorylcholine and cytidine diphosphocholine as well as two enzyme activities, a choline kinase and a cytidine diphosphocholine pyrophosphorylase, were identified in pneumococcal extracts. It is suggested that cytidine diphosphocholine may be a biosynthetic precursor of the choline moiety in the teichoic acids of pneumococcus. | Choline metabolism in pneumococci. Phosphorylcholine and cytidine diphosphocholine as well as two enzyme activities, a choline kinase and a cytidine diphosphocholine pyrophosphorylase, were identified in pneumococcal extracts. It is suggested that cytidine diphosphocholine may be a biosynthetic precursor of the choline moiety in the teichoic acids of pneumococcus. | [
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|
PMID:15989 | O-alkylhomoserine synthesis catalyzed by O-acetylhomoserine sulfhydrylase in microorganisms. | An enzyme that can synthesize O-alkylhomoserine from alcohols and O-acetylhomoserine was purified from Corynebacterium acetophilum. The enzyme was found to be identical to O-acetylhomoserine sulfhydrylase; a preparation that appeared homogeneous on polyacrylamide gel electrophoresis showed both O-alkylhomoserine-synthesizing and O-acetylhomoserine sulfhydrylase activities. Its molecular weight was determined to be about 220,000, and it consisted of two subunits. Its pH and temperature optima for the two reactions were the same. Besides catalyzing the formation of homocysteine from O-acetylhomoserine and sulfide, it also catalyzed the syntheses of O-alkylhomoserines corresponding to the alcohols added form O-acetylhomoserine and ethyl alcohol, n-propylalcohol, n-butyl alcohol, methyl alcohol, and n-pentyl alcohol, its activities with these alcohols decreasing in that order. L-Homoserine, O-succinylhomoserine, and O-acetylserine reacted with sulfide. O-ethylhomoserine, O-acetylthreonine, O-succinylhomoserine, and O-acetylserine inhibited both enzyme activities. O-acetylhomoserine sulfhydrylase purified from Saccharomyces cerevisiae also showed O-alkylhomoserine-synthesizing activity. Thus, O-acetylhomoserine sulfhydrylase seems to catalyze O-alkylhomoserine synthesis in the presence of appropriate concentrations of alcohol and O-acetylhomoserine in microorganisms. | O-alkylhomoserine synthesis catalyzed by O-acetylhomoserine sulfhydrylase in microorganisms. An enzyme that can synthesize O-alkylhomoserine from alcohols and O-acetylhomoserine was purified from Corynebacterium acetophilum. The enzyme was found to be identical to O-acetylhomoserine sulfhydrylase; a preparation that appeared homogeneous on polyacrylamide gel electrophoresis showed both O-alkylhomoserine-synthesizing and O-acetylhomoserine sulfhydrylase activities. Its molecular weight was determined to be about 220,000, and it consisted of two subunits. Its pH and temperature optima for the two reactions were the same. Besides catalyzing the formation of homocysteine from O-acetylhomoserine and sulfide, it also catalyzed the syntheses of O-alkylhomoserines corresponding to the alcohols added form O-acetylhomoserine and ethyl alcohol, n-propylalcohol, n-butyl alcohol, methyl alcohol, and n-pentyl alcohol, its activities with these alcohols decreasing in that order. L-Homoserine, O-succinylhomoserine, and O-acetylserine reacted with sulfide. O-ethylhomoserine, O-acetylthreonine, O-succinylhomoserine, and O-acetylserine inhibited both enzyme activities. O-acetylhomoserine sulfhydrylase purified from Saccharomyces cerevisiae also showed O-alkylhomoserine-synthesizing activity. Thus, O-acetylhomoserine sulfhydrylase seems to catalyze O-alkylhomoserine synthesis in the presence of appropriate concentrations of alcohol and O-acetylhomoserine in microorganisms. | [
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|
PMID:15990 | Alkaline structural transition of 4-nitrobenz-2-oxa-1,3-diazolyl-Lysozyme. Kinetic and spectroscopic investigations. | When lysozyme is reacted with 4-chloro-7-nitrobenz-2-oxa-1,3-diazole (NBD-CL), A 1:1 covalent product is produced, in which the NBD group arylates the phenolic hydroxyl group of Tyr-23 (Aboderin, A. A., and Boedefeld, E. (1976) Biochim. Biophys. Acta 420, 177). Changing the pH from neutral to alkaline conditions results in a large spectral shift of the absorption band associated with the NBD chromophore (Aboderin, A. A., Boedefeld, E., and Luisi, P. L. (1973) Biochim. Biophys. Acta 328, 30). In the present work it is shown that this spectral change is due to the formation of a sigma complex in which a hydroxyl ion is added to the aromatic nucleus of the nitrobenzoxadiazole system. Circular dichroic studies suggest that the NBD group is held in a conformationally rigid state in the protein. The kinetics of the spectral change accompanying the formation of the sigma complex has been investigated with a rapid mixing stopped flow spectrophotometer both in the modified enzyme and in the low molecular weight model compounds N-acetyl-(O-NBD)-L-tyrosinamide and glycyl-(O-NBD)-L-tyrosine. In the pH range from 10.1 to 12.7, the time course of the reaction is first order in the case of the modified enzyme (k = 4.8 s-1) and bimolecular and much slower (under pseudo-first order conditions) in the low molecular weight compounds. It is suggested that in the enzyme the reaction proceeds much faster because of the hydrophobic environment around the reacting groups. It is further suggested that the unimolecularity in the enzyme is due to a rate-determining isomerization step, probably connected with a local rearrangement of the protein conformation following the ionization of Tyr-20. | Alkaline structural transition of 4-nitrobenz-2-oxa-1,3-diazolyl-Lysozyme. Kinetic and spectroscopic investigations. When lysozyme is reacted with 4-chloro-7-nitrobenz-2-oxa-1,3-diazole (NBD-CL), A 1:1 covalent product is produced, in which the NBD group arylates the phenolic hydroxyl group of Tyr-23 (Aboderin, A. A., and Boedefeld, E. (1976) Biochim. Biophys. Acta 420, 177). Changing the pH from neutral to alkaline conditions results in a large spectral shift of the absorption band associated with the NBD chromophore (Aboderin, A. A., Boedefeld, E., and Luisi, P. L. (1973) Biochim. Biophys. Acta 328, 30). In the present work it is shown that this spectral change is due to the formation of a sigma complex in which a hydroxyl ion is added to the aromatic nucleus of the nitrobenzoxadiazole system. Circular dichroic studies suggest that the NBD group is held in a conformationally rigid state in the protein. The kinetics of the spectral change accompanying the formation of the sigma complex has been investigated with a rapid mixing stopped flow spectrophotometer both in the modified enzyme and in the low molecular weight model compounds N-acetyl-(O-NBD)-L-tyrosinamide and glycyl-(O-NBD)-L-tyrosine. In the pH range from 10.1 to 12.7, the time course of the reaction is first order in the case of the modified enzyme (k = 4.8 s-1) and bimolecular and much slower (under pseudo-first order conditions) in the low molecular weight compounds. It is suggested that in the enzyme the reaction proceeds much faster because of the hydrophobic environment around the reacting groups. It is further suggested that the unimolecularity in the enzyme is due to a rate-determining isomerization step, probably connected with a local rearrangement of the protein conformation following the ionization of Tyr-20. | [
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PMID:15991 | Resolution and partial characterization of two aldehyde reductases of mammalian liver. | Investigation of NADP-dependent aldehyde reductase activity in mouse liver led to the finding that two distinct reductases are separable by DE52 ion exchange chromatography. Aldehyde reductase I (AR I) appears in the effluent, while aldehyde reductase II (AR II) is eluted with a salt gradient. By several procedures AR II was purified over 1100-fold from liver supernatant fraction, but AR I could be pruified only 107-fold because of its instability. The two enzymes are different in regard to pH optimum, substrate specificity, response to inhibitors, and reactivity with antibody to AR II. While both enzymes utilize aromatic aldehydes well, only AR II ACTS ON D-glucuronate, indicating that it is the aldyhyde reductase recently reported to be identical to NADP-L-gulonate dehydrogenase. The presence of two NADP-linked aldehyde reductases in liver has apparently not heretofore been reported. | Resolution and partial characterization of two aldehyde reductases of mammalian liver. Investigation of NADP-dependent aldehyde reductase activity in mouse liver led to the finding that two distinct reductases are separable by DE52 ion exchange chromatography. Aldehyde reductase I (AR I) appears in the effluent, while aldehyde reductase II (AR II) is eluted with a salt gradient. By several procedures AR II was purified over 1100-fold from liver supernatant fraction, but AR I could be pruified only 107-fold because of its instability. The two enzymes are different in regard to pH optimum, substrate specificity, response to inhibitors, and reactivity with antibody to AR II. While both enzymes utilize aromatic aldehydes well, only AR II ACTS ON D-glucuronate, indicating that it is the aldyhyde reductase recently reported to be identical to NADP-L-gulonate dehydrogenase. The presence of two NADP-linked aldehyde reductases in liver has apparently not heretofore been reported. | [
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|
PMID:15992 | gamma-Glutamylcysteine synthetase. Further purification, "half of the sites" reactivity, subunits, and specificity. | gamma-Glutamylcysteine synthetase was purified from rat liver by an improved method involving chromatography on Sepharose-aminohexyl-ATP to a specific activity of about 1600 units/mg, or approximately twice that previously obtained; it is thus the most active preparation of this enzyme thus far isolated. The earlier preparation, which is homogeneous on polyacrylamide gel electrophoresis, exhibits "half of the sites" reactivity in that it binds a maximum of 0.5 mol of the inhibitor L-methionine-S-sulfoximine phosphate per mol of enzyme. In contrast, the present enzyme preparation binds 1 mol of methionine sulfoximine phosphate per mol of enzyme; it also differs from the enzyme obtained earlier in exhibiting much less ATPase activity and less activity in catalyzing ATP-dependent cyclization of glutamate. gamma-Glutamylcysteine synthetase dissociates in sodium dodecyl sulfate into two nonidentical subunits of apparent molecular weights 74,000 and 24,000; after cross-linking with dimethyl-suberimidate, a species having a molecular weight of about 100,000 was found on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. New information has been obtained about the interaction of the enzyme with glutamate analogs; thus, the enzyme is active with such glutamate analogs as beta-glutamate, N-methyl-L-glutamate, and threo-beta-hydroxy-L-glutanate, and it is effectively inhibited by cis-1-amino-1,3-dicarboxycyclonexane, 2-amino-4-phosphonobutyrate, and gamma-methylglutamate. | gamma-Glutamylcysteine synthetase. Further purification, "half of the sites" reactivity, subunits, and specificity. gamma-Glutamylcysteine synthetase was purified from rat liver by an improved method involving chromatography on Sepharose-aminohexyl-ATP to a specific activity of about 1600 units/mg, or approximately twice that previously obtained; it is thus the most active preparation of this enzyme thus far isolated. The earlier preparation, which is homogeneous on polyacrylamide gel electrophoresis, exhibits "half of the sites" reactivity in that it binds a maximum of 0.5 mol of the inhibitor L-methionine-S-sulfoximine phosphate per mol of enzyme. In contrast, the present enzyme preparation binds 1 mol of methionine sulfoximine phosphate per mol of enzyme; it also differs from the enzyme obtained earlier in exhibiting much less ATPase activity and less activity in catalyzing ATP-dependent cyclization of glutamate. gamma-Glutamylcysteine synthetase dissociates in sodium dodecyl sulfate into two nonidentical subunits of apparent molecular weights 74,000 and 24,000; after cross-linking with dimethyl-suberimidate, a species having a molecular weight of about 100,000 was found on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. New information has been obtained about the interaction of the enzyme with glutamate analogs; thus, the enzyme is active with such glutamate analogs as beta-glutamate, N-methyl-L-glutamate, and threo-beta-hydroxy-L-glutanate, and it is effectively inhibited by cis-1-amino-1,3-dicarboxycyclonexane, 2-amino-4-phosphonobutyrate, and gamma-methylglutamate. | [
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|
PMID:15993 | Covalent interaction of L-2-amino-4-oxo-5-chloropentanoate at glutamate binding site of gamma-glutamylcysteine synthetase. | gamma-Glutamylcysteine synthetase is inactivated by incubation with low concentrations of L-2-amino-4-oxo-5-chloropentanoate. Very low concentrations of magnesium ions or certain other divalent cations are required for inactivation. L-Glutamate, but not D-glutamate or L-glutamine, protected against inactivation and the protective effect of L-glutamate was increased in the presence of ATP or ADP. L-alpha-Aminobutyrate increased the rate of inactivation by the chloroketone. When the chloroketone was added to the dipeptide synthesis system, inhibition was competitive with L-glutamate. Iodoacetamide also inhibited the enzyme; however, this reagent is much less effective than the chloroketone and inhibition by iodoacetamide is less effectively prevented by L-glutamate. Studies with 14C-labeled chloroketone showed that this reagent binds stoichiometrically to the enzyme, and that it binds exclusively to its heavy subunit. | Covalent interaction of L-2-amino-4-oxo-5-chloropentanoate at glutamate binding site of gamma-glutamylcysteine synthetase. gamma-Glutamylcysteine synthetase is inactivated by incubation with low concentrations of L-2-amino-4-oxo-5-chloropentanoate. Very low concentrations of magnesium ions or certain other divalent cations are required for inactivation. L-Glutamate, but not D-glutamate or L-glutamine, protected against inactivation and the protective effect of L-glutamate was increased in the presence of ATP or ADP. L-alpha-Aminobutyrate increased the rate of inactivation by the chloroketone. When the chloroketone was added to the dipeptide synthesis system, inhibition was competitive with L-glutamate. Iodoacetamide also inhibited the enzyme; however, this reagent is much less effective than the chloroketone and inhibition by iodoacetamide is less effectively prevented by L-glutamate. Studies with 14C-labeled chloroketone showed that this reagent binds stoichiometrically to the enzyme, and that it binds exclusively to its heavy subunit. | [
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PMID:15994 | Isolation, crystallization, and properties of indolyl-3-alkane alpha-hydroxylase. A novel tryptophan-metabolizing enzyme. | Indolyl-3-alkane alpha-hydroxylase, a novel tryptophan-metabolizing enzyme, was prepared in crystalline form from soil isolate organism Pseudomonas XA. Emission spectroscopy and atomic absorption analyses of purified enzyme revealed the presence of iron (0.8 mol/mol of protein), and a number of observations supported the presence of heme prosthetic group (1.1 mol/mol of protein). The S20,w value of indolyl-3-alkane alpha-hydroxylase is 10.2 S, and the molecular weight by sedimentation equilibrium ultracentrifugation is 250,000. The E1%280 of the enzyme is 21, and the isoelectric point by isoelectric focusing on ampholine polyacrylamide gel plates is 4.8. The enzyme catalyzes hydroxylation on the side chain of a variety of 3-substituted indole compounds, including certain tryptophan-containing oligopeptides. The reaction product from tryptamine was identified by proton nuclear magnetic resonance and gas chromatography/mass spectroscopy analyses. While the indole ring remained intact, hydroxylation occurred at the side chain carbon adjacent to the ring. Nuclear magnetic resonance studies indicated that hydroxylation always took place at the same position when the substrate was tryptophan methyl ester, tryptophol, indole-3-propionate, or indole-3-butyrate. No other chemical change occurred when these substrates were incubated with the enzyme. The Km value of indolyl-3-alkane alpha-hydroxylase for L-tryptophan is 2.4 X 10(-6) M, at pH 7.2. The enzyme is inhibited by potassium cyanide (0.1 mM) or hydroxylamine (1mM), but not by NaBH4 (25 mM), aminooxyacetic acid (7mM), quinacrine (1 mM), chlortetracycline (1 mM), p-mercuribenzoate (0.1 mM), or ethylenediaminetetraacetate (1 mM). The plasma half-life (t1/2) of indolyl-3-alkane alpha-hydroxylase in tumor-bearing mice is approximately 25 h. | Isolation, crystallization, and properties of indolyl-3-alkane alpha-hydroxylase. A novel tryptophan-metabolizing enzyme. Indolyl-3-alkane alpha-hydroxylase, a novel tryptophan-metabolizing enzyme, was prepared in crystalline form from soil isolate organism Pseudomonas XA. Emission spectroscopy and atomic absorption analyses of purified enzyme revealed the presence of iron (0.8 mol/mol of protein), and a number of observations supported the presence of heme prosthetic group (1.1 mol/mol of protein). The S20,w value of indolyl-3-alkane alpha-hydroxylase is 10.2 S, and the molecular weight by sedimentation equilibrium ultracentrifugation is 250,000. The E1%280 of the enzyme is 21, and the isoelectric point by isoelectric focusing on ampholine polyacrylamide gel plates is 4.8. The enzyme catalyzes hydroxylation on the side chain of a variety of 3-substituted indole compounds, including certain tryptophan-containing oligopeptides. The reaction product from tryptamine was identified by proton nuclear magnetic resonance and gas chromatography/mass spectroscopy analyses. While the indole ring remained intact, hydroxylation occurred at the side chain carbon adjacent to the ring. Nuclear magnetic resonance studies indicated that hydroxylation always took place at the same position when the substrate was tryptophan methyl ester, tryptophol, indole-3-propionate, or indole-3-butyrate. No other chemical change occurred when these substrates were incubated with the enzyme. The Km value of indolyl-3-alkane alpha-hydroxylase for L-tryptophan is 2.4 X 10(-6) M, at pH 7.2. The enzyme is inhibited by potassium cyanide (0.1 mM) or hydroxylamine (1mM), but not by NaBH4 (25 mM), aminooxyacetic acid (7mM), quinacrine (1 mM), chlortetracycline (1 mM), p-mercuribenzoate (0.1 mM), or ethylenediaminetetraacetate (1 mM). The plasma half-life (t1/2) of indolyl-3-alkane alpha-hydroxylase in tumor-bearing mice is approximately 25 h. | [
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|
PMID:15995 | Crystalline hemoprotein from Pseudomonas that catalyzes oxidation of side chain of tryptophan and other indole derivatives. | A new enzyme which catalyzes the oxidation of the side chain of tryptophan and other indole derivatives, has been purified to apparent homogeneity from Pseudomonas and crystallized. The overall purification was about 25-fold with a yield of 4.5%. The purified enzyme was apparently homogeneous as judged by polyacrylamide gel electrophoresis. The molecular weight estimated by gel filtration was approximately 280,000 and sedimentation coefficient (S20,w) was 11 by sucrose density gradient ultracentrifugation. The absorption spectra indicated that the enzyme was a hemoprotein. The purified enzyme was shown to catalyze the reaction in which 1 mol each of NH3 and CO2 was formed at the expense of 1 mol each of L-tryptophan and molecular oxygen. Neither peroxidase nor catalase activity was detected in the purified enzyme and no formation of H2O2 was observed during the enzyme reaction. The product(s) of the reaction was unstable but was converted to and was identified as its stable quinoxaline derivative, 2-(3-indolyl)quinoxaline, in the presence of o-phenylenediamine. These results indicate that the product of the reaction was 3-indolylglycoaldehyde or 3-indolylglyoxal. A variety of other indole derivatives such as D-tryptophan, 5-hydroxyl-L-tryptophan, tryptamine, serotonin, melatonin, N-acetyl-L-tryptophan, N-acetyl-L-tryptophanamide, 3-indoleacetamide, 3-indolelactic acid, 3-indolepropionic acid, 3-indoleethanol, and skatole were also substrates. | Crystalline hemoprotein from Pseudomonas that catalyzes oxidation of side chain of tryptophan and other indole derivatives. A new enzyme which catalyzes the oxidation of the side chain of tryptophan and other indole derivatives, has been purified to apparent homogeneity from Pseudomonas and crystallized. The overall purification was about 25-fold with a yield of 4.5%. The purified enzyme was apparently homogeneous as judged by polyacrylamide gel electrophoresis. The molecular weight estimated by gel filtration was approximately 280,000 and sedimentation coefficient (S20,w) was 11 by sucrose density gradient ultracentrifugation. The absorption spectra indicated that the enzyme was a hemoprotein. The purified enzyme was shown to catalyze the reaction in which 1 mol each of NH3 and CO2 was formed at the expense of 1 mol each of L-tryptophan and molecular oxygen. Neither peroxidase nor catalase activity was detected in the purified enzyme and no formation of H2O2 was observed during the enzyme reaction. The product(s) of the reaction was unstable but was converted to and was identified as its stable quinoxaline derivative, 2-(3-indolyl)quinoxaline, in the presence of o-phenylenediamine. These results indicate that the product of the reaction was 3-indolylglycoaldehyde or 3-indolylglyoxal. A variety of other indole derivatives such as D-tryptophan, 5-hydroxyl-L-tryptophan, tryptamine, serotonin, melatonin, N-acetyl-L-tryptophan, N-acetyl-L-tryptophanamide, 3-indoleacetamide, 3-indolelactic acid, 3-indolepropionic acid, 3-indoleethanol, and skatole were also substrates. | [
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|
PMID:15996 | Enzymatic conversion of bilirubin monoglucuronide to diglucuronide by rat liver plasma membranes. | Formation of bilirubin monoglucuronide from unconjugated bilirubin requires a microsomal enzyme, UDP-glucuronate glucuronyltransferase (EC 2.4.1.17). Conversion of bilirubin monoglucuronide to bilirubin diglucuronide, the major bilirubin conjugate in bile, was studied in subcellular fractions of rat liver. The highest specific activity for bilirubin diglucuronide formation occurred in a fraction highly enriched in plasma membranes. Studies of reaction stoichiometry and utilization of UDP-D-[14C]glucuronic acid revealed that conversion of bilirubin monoglucuronide to bilirubin diglucuronide is not catalyzed by UDP-glucuronyltransferase, and results from transglucuronidation of bilirubin monoglucuronide, with formation of bilirubin diglucuronide and unconjugated bilirubin. When unconjugated bilirubin was infused intravenously into rats at rates exceeding the maximal hepatic excretory capacity, bilirubin monoglucuronide accumulated in serum and bilirubin diglucuronide was found exclusively in bile as the predominant bilirubin metabolite. These results suggest that formation of bilirubin diglucuronide occurs at the surface membrane of the liver cell. Conversion of bilirubin monoglucuronide to bilirubin diglucuronide may play a role in the transport of bilirubin glucuronides from liver to bile. | Enzymatic conversion of bilirubin monoglucuronide to diglucuronide by rat liver plasma membranes. Formation of bilirubin monoglucuronide from unconjugated bilirubin requires a microsomal enzyme, UDP-glucuronate glucuronyltransferase (EC 2.4.1.17). Conversion of bilirubin monoglucuronide to bilirubin diglucuronide, the major bilirubin conjugate in bile, was studied in subcellular fractions of rat liver. The highest specific activity for bilirubin diglucuronide formation occurred in a fraction highly enriched in plasma membranes. Studies of reaction stoichiometry and utilization of UDP-D-[14C]glucuronic acid revealed that conversion of bilirubin monoglucuronide to bilirubin diglucuronide is not catalyzed by UDP-glucuronyltransferase, and results from transglucuronidation of bilirubin monoglucuronide, with formation of bilirubin diglucuronide and unconjugated bilirubin. When unconjugated bilirubin was infused intravenously into rats at rates exceeding the maximal hepatic excretory capacity, bilirubin monoglucuronide accumulated in serum and bilirubin diglucuronide was found exclusively in bile as the predominant bilirubin metabolite. These results suggest that formation of bilirubin diglucuronide occurs at the surface membrane of the liver cell. Conversion of bilirubin monoglucuronide to bilirubin diglucuronide may play a role in the transport of bilirubin glucuronides from liver to bile. | [
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|
PMID:15997 | Effect of concanavalin A on tyrosine aminotransferase in rat hepatoma tissue culture cells. Rapid reversible inactivation of soluble enzyme. | Concanavalin A added to intact cells at 37 degrees caused rapid and reversible inactivation of a soluble enzyme, tyrosine aminotransferase, in two lines of rat hepatoma tissue culture cells grown in monolayer culture. This temperature-dependent process was independent of de novo protein and RNA synthesis and independent of increased uptake of Ca2+ and Mg2+ or glucose. The inactivation could be reversed by adding alpha-methyl-D-mannopyranoside a competing sugar for concanavalin A binding. Other lectins known to bind to different sugars did not bring about the inactivation of tyrosine aminotransferase. Addition of concanavalin A did not result in the inactivation of another soluble enzyme, lactic dehydrogenase. The maintenance of tyrosine aminotransferase in an inactive form after the binding of concanavalin A to the cells required the continued presence of concanavalin A. This effect of concanavalin A could not be mimicked either by dibutyryl cyclic adenosine or guanosine monophosphoric acid. Incubation of cell extracts with concanavalin A did not result in inactivation nor did mixing of extracts from concanavalin A-treated cells with extracts from untreated cells. On the basis of these results we conclude that the following are the essential requirements for concanavalin A to bring about the inactivation of tyrosine aminotransferase: (a) the binding of native concanavalin A to the cells; (b) integrity of certain structural elements of the cells. | Effect of concanavalin A on tyrosine aminotransferase in rat hepatoma tissue culture cells. Rapid reversible inactivation of soluble enzyme. Concanavalin A added to intact cells at 37 degrees caused rapid and reversible inactivation of a soluble enzyme, tyrosine aminotransferase, in two lines of rat hepatoma tissue culture cells grown in monolayer culture. This temperature-dependent process was independent of de novo protein and RNA synthesis and independent of increased uptake of Ca2+ and Mg2+ or glucose. The inactivation could be reversed by adding alpha-methyl-D-mannopyranoside a competing sugar for concanavalin A binding. Other lectins known to bind to different sugars did not bring about the inactivation of tyrosine aminotransferase. Addition of concanavalin A did not result in the inactivation of another soluble enzyme, lactic dehydrogenase. The maintenance of tyrosine aminotransferase in an inactive form after the binding of concanavalin A to the cells required the continued presence of concanavalin A. This effect of concanavalin A could not be mimicked either by dibutyryl cyclic adenosine or guanosine monophosphoric acid. Incubation of cell extracts with concanavalin A did not result in inactivation nor did mixing of extracts from concanavalin A-treated cells with extracts from untreated cells. On the basis of these results we conclude that the following are the essential requirements for concanavalin A to bring about the inactivation of tyrosine aminotransferase: (a) the binding of native concanavalin A to the cells; (b) integrity of certain structural elements of the cells. | [
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|
PMID:15998 | Selective association of spectrin with the cytoplasmic surface of human erythrocyte plasma membranes. Quantitative determination with purified (32P)spectrin. | A specific association between spectrin and the inner surface of the human erythrocyte membrane has been examined by measuring the binding of purified [32P]spectrin to inside out, spectrin-depleted vesicles and to right side out ghost vesicles. Spectrin was labeled by incubating erythrocytes with 32Pi, and eluted from the ghost membranes by extraction in 0.3 mM NaPO4, pH 7.6. [32P]Spectrin was separated from actin and other proteins and isolated in a nonaggregated state as a So20,w = 7 S (in 0.3 mM NaPO4) or So20,w = 8 S (in 20 mM KCl, 0.3 mM NaPO4) protein after sedimentation on linear sucrose gradients. Binding of [32P]spectrin to inverted vesicles devoid of spectrin and actin was at least 10-fold greater than to right side out membranes, and exhibited different properties. Association with inside out vesicles was slow, was decreased to the value for right side out vesicles at high pH, or after heating spectrin above 50 degrees prior to assay, and was saturable with increasing levels of spectrin. Binding to everted vesicles was rapid, unaffected by pH or by heating spectrin, and rose linearly with the concentration of spectrin. Scatchard plots of binding to inverted vesicles were linear at pH 7.6, with a KD of 45 microng/ml, while at pH 6.6, plots were curvilinear and consistent with two types of interactions with a KD of 4 and 19 microng/ml, respectively. The maximal binding capacity at both pH values was about 200 microng of spectrin/mg of membrane protein. Unlabeled spectrin competed for binding with 50% displacement at 27 microng/ml. [32P]Spectrin dissociated and associated with inverted vesicles with an identical dependence on ionic strength as observed for elution of native spectrin from ghosts. MgCl2, CaCl2 (1 to 4 mM) and EDTA (0.5 to 1 mM) had little effect on binding in the presence of 20 mM KCl, while at low ionic strength, MgCl2 (1 mM) increased binding and inhibited dissociation to the same extent as 10 to 20 mM KCl. Binding was abolished by pretreatment of vesicles with 0.1 M acetic acid, or with 0.1 microng/ml of trypsin. The periodic acid-Schiff-staining bands were unaffected by trypsin digestion which destroyed binding; mild digestion, which decreased binding only 50%, converted Band 3 almost completely to a membrane-bound 50,000-dalton fragment resistant to further proteolysis. These experiments suggest that attachment of spectrin to the cytoplasmic surface of the membrane results from a selective protein-protein interaction which is independent of erythrocyte actin. A direct role of the major sialoglycoprotein or Band 3 as a membrane binding site appears unlikely. | Selective association of spectrin with the cytoplasmic surface of human erythrocyte plasma membranes. Quantitative determination with purified (32P)spectrin. A specific association between spectrin and the inner surface of the human erythrocyte membrane has been examined by measuring the binding of purified [32P]spectrin to inside out, spectrin-depleted vesicles and to right side out ghost vesicles. Spectrin was labeled by incubating erythrocytes with 32Pi, and eluted from the ghost membranes by extraction in 0.3 mM NaPO4, pH 7.6. [32P]Spectrin was separated from actin and other proteins and isolated in a nonaggregated state as a So20,w = 7 S (in 0.3 mM NaPO4) or So20,w = 8 S (in 20 mM KCl, 0.3 mM NaPO4) protein after sedimentation on linear sucrose gradients. Binding of [32P]spectrin to inverted vesicles devoid of spectrin and actin was at least 10-fold greater than to right side out membranes, and exhibited different properties. Association with inside out vesicles was slow, was decreased to the value for right side out vesicles at high pH, or after heating spectrin above 50 degrees prior to assay, and was saturable with increasing levels of spectrin. Binding to everted vesicles was rapid, unaffected by pH or by heating spectrin, and rose linearly with the concentration of spectrin. Scatchard plots of binding to inverted vesicles were linear at pH 7.6, with a KD of 45 microng/ml, while at pH 6.6, plots were curvilinear and consistent with two types of interactions with a KD of 4 and 19 microng/ml, respectively. The maximal binding capacity at both pH values was about 200 microng of spectrin/mg of membrane protein. Unlabeled spectrin competed for binding with 50% displacement at 27 microng/ml. [32P]Spectrin dissociated and associated with inverted vesicles with an identical dependence on ionic strength as observed for elution of native spectrin from ghosts. MgCl2, CaCl2 (1 to 4 mM) and EDTA (0.5 to 1 mM) had little effect on binding in the presence of 20 mM KCl, while at low ionic strength, MgCl2 (1 mM) increased binding and inhibited dissociation to the same extent as 10 to 20 mM KCl. Binding was abolished by pretreatment of vesicles with 0.1 M acetic acid, or with 0.1 microng/ml of trypsin. The periodic acid-Schiff-staining bands were unaffected by trypsin digestion which destroyed binding; mild digestion, which decreased binding only 50%, converted Band 3 almost completely to a membrane-bound 50,000-dalton fragment resistant to further proteolysis. These experiments suggest that attachment of spectrin to the cytoplasmic surface of the membrane results from a selective protein-protein interaction which is independent of erythrocyte actin. A direct role of the major sialoglycoprotein or Band 3 as a membrane binding site appears unlikely. | [
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PMID:15999 | Thyroid hormone regulation of beta-adrenergic receptor number. | The effects of exogenous thyroid hormones (thyroxine and triiodothyronine) on beta-adrenergic receptors in the rat myocardium were investigated. The potent beta-adrenergic antagonist, (-)-[3H]dihydroalprenolol, was used to directly estimate the number and affinity of beta-adrenergic receptors in rat heart membranes from control and hyperthyroid rats. Cardiac membranes from hyperthyroid rats contained 196 +/- 7 fmol of (-)-[3H]dihydroalprenolol binding sites/mg of protein which was significantly (p less than 0.005) greater than the number of binding sites (89 +/- 5 fmol/mg of protein) present in control membranes. The equilibrium dissociation constant (KD) for the interaction of receptors with dihydroalprenolol was the same (2 to 15 nM) in membranes from control and hyperthyroid rats. Similarly, there was no significant difference between the control and hyperthyroid membranes in the affinity of the beta-adrenergic receptor binding sites for the beta-adrenergic agonist isoproterenol. The results of this study demonstrate that thyroid hormones can regulate the number of cardiac beta-adrenergic receptors. The increased numbers of receptors may be responsible, at least in part, for the enhanced catecholamine sensitivity of beta-adrenergic-coupled cardiac responses in the hyperthyroid state. | Thyroid hormone regulation of beta-adrenergic receptor number. The effects of exogenous thyroid hormones (thyroxine and triiodothyronine) on beta-adrenergic receptors in the rat myocardium were investigated. The potent beta-adrenergic antagonist, (-)-[3H]dihydroalprenolol, was used to directly estimate the number and affinity of beta-adrenergic receptors in rat heart membranes from control and hyperthyroid rats. Cardiac membranes from hyperthyroid rats contained 196 +/- 7 fmol of (-)-[3H]dihydroalprenolol binding sites/mg of protein which was significantly (p less than 0.005) greater than the number of binding sites (89 +/- 5 fmol/mg of protein) present in control membranes. The equilibrium dissociation constant (KD) for the interaction of receptors with dihydroalprenolol was the same (2 to 15 nM) in membranes from control and hyperthyroid rats. Similarly, there was no significant difference between the control and hyperthyroid membranes in the affinity of the beta-adrenergic receptor binding sites for the beta-adrenergic agonist isoproterenol. The results of this study demonstrate that thyroid hormones can regulate the number of cardiac beta-adrenergic receptors. The increased numbers of receptors may be responsible, at least in part, for the enhanced catecholamine sensitivity of beta-adrenergic-coupled cardiac responses in the hyperthyroid state. | [
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|
PMID:16000 | Effects of GTP on binding of (3H) glucagon to receptors in rat hepatic plasma membranes. | In this study, we report the preparation of [3H]glucagon and its characteristics of binding to receptors in the rat liver plasma membrane. Binding of the labeled hormone is optimal at pH 7.0. In the absence of GTP, [3H]glucagon binding to receptors is slow and the time of equilibration is inversely proportional to the hormone concentration. In the presence of GTP, equilibrium is reached within 30 s regardless of hormone levels, and the kinetics of binding are in accord with the kinetics of activation of adenylate cyclase by native glucagon in the presence of the nucleotide. Equilibrium binding measurements indicate that, in the absence of GTP, the binding isotherm is sigmoidal with an apparent Kd of 2 nM. The addition of GTP results in a complex binding isotherm with about 90% of the binding sites having a considerably lower apparent dissociation constant (greater than 10 nM) and a small population of sites having high affinity for the hormone. The binding properties of [3H]glucagon are compared with those of 125I-glucagon, and the implications of the actions of GTP on glucagon binding are discussed in relation to the overall regulation of adenylate cyclase by hormone and the nucleotide. | Effects of GTP on binding of (3H) glucagon to receptors in rat hepatic plasma membranes. In this study, we report the preparation of [3H]glucagon and its characteristics of binding to receptors in the rat liver plasma membrane. Binding of the labeled hormone is optimal at pH 7.0. In the absence of GTP, [3H]glucagon binding to receptors is slow and the time of equilibration is inversely proportional to the hormone concentration. In the presence of GTP, equilibrium is reached within 30 s regardless of hormone levels, and the kinetics of binding are in accord with the kinetics of activation of adenylate cyclase by native glucagon in the presence of the nucleotide. Equilibrium binding measurements indicate that, in the absence of GTP, the binding isotherm is sigmoidal with an apparent Kd of 2 nM. The addition of GTP results in a complex binding isotherm with about 90% of the binding sites having a considerably lower apparent dissociation constant (greater than 10 nM) and a small population of sites having high affinity for the hormone. The binding properties of [3H]glucagon are compared with those of 125I-glucagon, and the implications of the actions of GTP on glucagon binding are discussed in relation to the overall regulation of adenylate cyclase by hormone and the nucleotide. | [
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PMID:16001 | Endonuclease from Escherichia coli that acts specifically upon duplex DNA damaged by ultraviolet light, osmium tetroxide, acid, or x-rays. | An endonuclease which is active upon DNA exposed to ultraviolet light at a photoproduct other than thymine dimers has been extensively purified from Escherichia coli. The small (2.7 S) enzyme is active in the presence of EDTA, has a neutral pH optimum, and is inhibited by tRNA and 1 M NaCl. It has no detectable exonuclease, DNA-N-glycosidase, or ribonuclease activities. The enzyme also nicks duplex DNA exposed to OsO4, x-rays, or acid, but it does not act upon undamaged DNA or irradiated single-stranded DNA. The majority of sites of action in DNA exposed to ultraviolet light or OsO4 appear to be alkali-stable, but those in DNA exposed to x-rays or acid are not. The incisions created by the endonuclease contain 5'-phosphate termini. The enzyme is possibly the same as E. coli endonuclease III described by Radman (Radman, M. (1976) J. Biol. Chem. 251, 1438-1445), but it is distinguishable from the other endodeoxyribonucleases described from that organism. | Endonuclease from Escherichia coli that acts specifically upon duplex DNA damaged by ultraviolet light, osmium tetroxide, acid, or x-rays. An endonuclease which is active upon DNA exposed to ultraviolet light at a photoproduct other than thymine dimers has been extensively purified from Escherichia coli. The small (2.7 S) enzyme is active in the presence of EDTA, has a neutral pH optimum, and is inhibited by tRNA and 1 M NaCl. It has no detectable exonuclease, DNA-N-glycosidase, or ribonuclease activities. The enzyme also nicks duplex DNA exposed to OsO4, x-rays, or acid, but it does not act upon undamaged DNA or irradiated single-stranded DNA. The majority of sites of action in DNA exposed to ultraviolet light or OsO4 appear to be alkali-stable, but those in DNA exposed to x-rays or acid are not. The incisions created by the endonuclease contain 5'-phosphate termini. The enzyme is possibly the same as E. coli endonuclease III described by Radman (Radman, M. (1976) J. Biol. Chem. 251, 1438-1445), but it is distinguishable from the other endodeoxyribonucleases described from that organism. | [
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PMID:16002 | A new endonuclease from Escherichia coli acting at apurinic sites in DNA. | A new DNA endonuclease has been purified 3000-fold from Escherichia coli. The enzyme specifically catalyzes the formation of single strand breaks at apurinic and apyrimidinic sites in DNA, but has no activity on intact or single-stranded DNA. Further, the enzyme shows little or no activity on heavily ultraviolet-irradiated DNA, but cleaves x-irradiated DNA, presumably at apurinic and apyrimidinic sites introduced by the radiation treatment. The enzyme, which is tentatively named endonuclease IV, has no detectable associated exonuclease or DNA N-glycosidase activity and does not seem to be identical with any previously known E. coli endonuclease. Endonuclease IV has no Mg2+ requirement, and is fully active in the presence of EDTA. Enzyme activity is stimulated by 0.2 to 0.3 M NaCl and is unusually salt-resistant. Further, the enzyme is fairly heat-stable, and is not inhibited by tRNA. The sidimentation coefficient, S(o)20,w, is 3.4 S. It seems that endonuclease IV is active in DNA repair. | A new endonuclease from Escherichia coli acting at apurinic sites in DNA. A new DNA endonuclease has been purified 3000-fold from Escherichia coli. The enzyme specifically catalyzes the formation of single strand breaks at apurinic and apyrimidinic sites in DNA, but has no activity on intact or single-stranded DNA. Further, the enzyme shows little or no activity on heavily ultraviolet-irradiated DNA, but cleaves x-irradiated DNA, presumably at apurinic and apyrimidinic sites introduced by the radiation treatment. The enzyme, which is tentatively named endonuclease IV, has no detectable associated exonuclease or DNA N-glycosidase activity and does not seem to be identical with any previously known E. coli endonuclease. Endonuclease IV has no Mg2+ requirement, and is fully active in the presence of EDTA. Enzyme activity is stimulated by 0.2 to 0.3 M NaCl and is unusually salt-resistant. Further, the enzyme is fairly heat-stable, and is not inhibited by tRNA. The sidimentation coefficient, S(o)20,w, is 3.4 S. It seems that endonuclease IV is active in DNA repair. | [
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|
PMID:16003 | Characterization of the m7G(5')pppN-pyrophosphatase activity from HeLa cells. | The m7(G(5')pppN-pyrophosphatase activity previously detected in HeLa cells has been further characterized. Results from DEAE-cellulose column chromatography and polyacrylamide gel electrophoresis under nondenaturing conditions revealed only one enzyme activity in HeLa cell extracts which was capable of selectively hydrolyzing m7G(5')pppN to yield m7pG + ppN (where N = 2'-O-methylated or unmethylated ribonucleosides or oligonucleotides of up to 8 to 10 nucleosides in length). The majority (approximately 95%) of this activity was found in the cytoplasmic extract but appeared not to be associated with the lysosomal fraction. m7G(5')pppG was hydrolyzed by the partially purified enzyme in the absence of divalent cations at a pH optimum of 7.5 and a temperature optimum of 45 degrees, with a Michaelis constant (Km) of 1.7 micronM. Sedimentation analysis and gel filtration showed the molecular weight of the enzyme as approximately 81,000. Inhibition studies testing the effect of a number of prospective substrates on the rate of m7G(5')pppG hydrolysis have confirmed the importance of the methyl moiety at the N7 position of guanosine for enzyme-substrate interaction. Furthermore, the trimethylated guanosine-containing 5'-terminal structure derived from U-2 RNA was found not to serve as substrate, and 7-methylinosine, unlike 7-methylguanosine, was not an effective inhibitor of m7G(5')pppG hydrolysis. Thus, the 2-amino group of the 7-methylguanosine portion of m7G(5')pppN is also important for substrate interaction with this specific pyrophosphatase. | Characterization of the m7G(5')pppN-pyrophosphatase activity from HeLa cells. The m7(G(5')pppN-pyrophosphatase activity previously detected in HeLa cells has been further characterized. Results from DEAE-cellulose column chromatography and polyacrylamide gel electrophoresis under nondenaturing conditions revealed only one enzyme activity in HeLa cell extracts which was capable of selectively hydrolyzing m7G(5')pppN to yield m7pG + ppN (where N = 2'-O-methylated or unmethylated ribonucleosides or oligonucleotides of up to 8 to 10 nucleosides in length). The majority (approximately 95%) of this activity was found in the cytoplasmic extract but appeared not to be associated with the lysosomal fraction. m7G(5')pppG was hydrolyzed by the partially purified enzyme in the absence of divalent cations at a pH optimum of 7.5 and a temperature optimum of 45 degrees, with a Michaelis constant (Km) of 1.7 micronM. Sedimentation analysis and gel filtration showed the molecular weight of the enzyme as approximately 81,000. Inhibition studies testing the effect of a number of prospective substrates on the rate of m7G(5')pppG hydrolysis have confirmed the importance of the methyl moiety at the N7 position of guanosine for enzyme-substrate interaction. Furthermore, the trimethylated guanosine-containing 5'-terminal structure derived from U-2 RNA was found not to serve as substrate, and 7-methylinosine, unlike 7-methylguanosine, was not an effective inhibitor of m7G(5')pppG hydrolysis. Thus, the 2-amino group of the 7-methylguanosine portion of m7G(5')pppN is also important for substrate interaction with this specific pyrophosphatase. | [
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PMID:16004 | Detection of multiple forms of rat liver ornithine decarboxylase. | Rat liver ornithine decarboxylase induced by injection of thioacetamide has been separated into at least two fractions by covalent chromatography on an activated thiol-Sepharose 4B column. The two major fractions could be distinguished by ion exchange chromatography and electrophoresis on acrylamide gels. In addition, the two forms displayed different Km values for ornithine. Although the two forms are separable, they display identical antigenic properties, pH optima, and they appear to be the same molecular size. The biological significance or the relationship between multiple forms of ornithine decarboxylase is not understood. | Detection of multiple forms of rat liver ornithine decarboxylase. Rat liver ornithine decarboxylase induced by injection of thioacetamide has been separated into at least two fractions by covalent chromatography on an activated thiol-Sepharose 4B column. The two major fractions could be distinguished by ion exchange chromatography and electrophoresis on acrylamide gels. In addition, the two forms displayed different Km values for ornithine. Although the two forms are separable, they display identical antigenic properties, pH optima, and they appear to be the same molecular size. The biological significance or the relationship between multiple forms of ornithine decarboxylase is not understood. | [
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|
PMID:16005 | Production of monospecific antibodies to rat liver ornithine decarboxylase and their use in turnover studies. | Two forms of ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) were purified from the livers of rats which had been treated with thioacetamide for 16 h (for details, see miniprint to Obenrader, M.F., and Prouty, W. F. (1977) J. Biol. Chem. 252, 2860-2865). The enzyme was purified over 7,000-fold from liver cytosol with an overall yield of 8%. Enzyme activity was eluted finally in two distinct fractions by chromatography on activated thiol-Sepharose 4B. Both forms appear to be dimeric proteins having molecular weights of approximately 100,000 by equilibrium sedimentation and analysis on a calibrated Sephadex G-200 column. The apparent subunits are approximately 50,000 daltons as determined by electrophoresis on polyacrylamide gels in the presence of sodium dodecyl sulfate. Since electrophoresis in the presence of detergent is the only method used here to indicate subunits, the possibility that conditions of sample preparation resulted in splitting of a labile protein cannot be excluded from consideration. Ornithine decarboxylase has a very broad pH-activity curve with an optimum that shifts from pH 7.0 to pH 7.8 as the enzyme is purified. The apparent Km values for a highly purified mixture of the two forms of enzyme for L-ornithine and pyridoxal 5'-phosphate were determined to be 0.13 mM and 0.25 micronM, respectively. Both sodium and potassium chloride were shown to inhibit enzymatic activity; 50% inhibition occurred at 270 mM for each when Km amounts or ornithine were used. Rat liver ornithine decarboxylase antiserum was prepared in rabbits using Form I of the enzyme as the antigen. The antibody was shown to precipitate quantitatively the ornithine decarboxylase activity isolated from induced rat liver and rat ventral prostate. The specificity of the antiserum was demonstrated by rocket immunoelectrophoresis and by gel electrophoresis in the presence of sodium dodecyl sulfate using immunoprecipitates obtained from enzyme preparations labeled either in vivo, with [3H]leucine, or in vitro, by reductive methylation using formaldehyde and sodium [3H]borohydride. The antibody preparation has been used in a titration method to assess the half-life of antigen in livers of rats induced for ornithine decarboxylase by injection of thioacetamide. In two experiments, the t1/2 of activity at the height of induction, following injection of cycloheximide, was 19 and 24 min, while the t1/2 of disappearance of antigen was 28 and 33 min, respectively. In each experiment the t1/2 for antigen was significantly longer than the t1/2 for loss of enzyme activity. Enzyme levels appear to be modulated primarily by synthesis and degradation of antigen. Furthermore, the observation that enzyme activity is lost with a shorter t1/2 than antigen is consistent with the idea that denaturation is an initial step in the degradation of this enzyme... | Production of monospecific antibodies to rat liver ornithine decarboxylase and their use in turnover studies. Two forms of ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) were purified from the livers of rats which had been treated with thioacetamide for 16 h (for details, see miniprint to Obenrader, M.F., and Prouty, W. F. (1977) J. Biol. Chem. 252, 2860-2865). The enzyme was purified over 7,000-fold from liver cytosol with an overall yield of 8%. Enzyme activity was eluted finally in two distinct fractions by chromatography on activated thiol-Sepharose 4B. Both forms appear to be dimeric proteins having molecular weights of approximately 100,000 by equilibrium sedimentation and analysis on a calibrated Sephadex G-200 column. The apparent subunits are approximately 50,000 daltons as determined by electrophoresis on polyacrylamide gels in the presence of sodium dodecyl sulfate. Since electrophoresis in the presence of detergent is the only method used here to indicate subunits, the possibility that conditions of sample preparation resulted in splitting of a labile protein cannot be excluded from consideration. Ornithine decarboxylase has a very broad pH-activity curve with an optimum that shifts from pH 7.0 to pH 7.8 as the enzyme is purified. The apparent Km values for a highly purified mixture of the two forms of enzyme for L-ornithine and pyridoxal 5'-phosphate were determined to be 0.13 mM and 0.25 micronM, respectively. Both sodium and potassium chloride were shown to inhibit enzymatic activity; 50% inhibition occurred at 270 mM for each when Km amounts or ornithine were used. Rat liver ornithine decarboxylase antiserum was prepared in rabbits using Form I of the enzyme as the antigen. The antibody was shown to precipitate quantitatively the ornithine decarboxylase activity isolated from induced rat liver and rat ventral prostate. The specificity of the antiserum was demonstrated by rocket immunoelectrophoresis and by gel electrophoresis in the presence of sodium dodecyl sulfate using immunoprecipitates obtained from enzyme preparations labeled either in vivo, with [3H]leucine, or in vitro, by reductive methylation using formaldehyde and sodium [3H]borohydride. The antibody preparation has been used in a titration method to assess the half-life of antigen in livers of rats induced for ornithine decarboxylase by injection of thioacetamide. In two experiments, the t1/2 of activity at the height of induction, following injection of cycloheximide, was 19 and 24 min, while the t1/2 of disappearance of antigen was 28 and 33 min, respectively. In each experiment the t1/2 for antigen was significantly longer than the t1/2 for loss of enzyme activity. Enzyme levels appear to be modulated primarily by synthesis and degradation of antigen. Furthermore, the observation that enzyme activity is lost with a shorter t1/2 than antigen is consistent with the idea that denaturation is an initial step in the degradation of this enzyme... | [
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|
PMID:16006 | Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase. | Beef heart mitochondrial ATPase (F1) exhibited a single binding site for Pi. The interaction with Pi was reversible, partially dependent on the presence of divalent metal ions, and characterized by a dissociation constant at pH 7.5 of 80 micronM. A variety of substances known to influence oxidative phosphorylation or the activity of the soluble ATPase (F1) also influenced Pi binding by the enzyme. Thus aurovertin, an inhibitor of oxidative phosphorylation, which was bound tightly by F1 and inhibited ATPase activity, enhanced Pi binding via a 4-fold increase in the affinity of the enzyme for Pi (KD = 20 micronM) but did not alter binding stoichiometry. Anions such as SO4(2-), SO3(2-), chromate, and 2,4-dinitrophenolate, which stimulated ATPase activity of F1, also enhanced Pi binding. Inhibitors of ATPase activity such as nickel/bathophenanthroline and the protein ATPase inhibitor of Pullman and Monroy (Pullman, M. E., and Monroy, G. C. (1963) J. Biol. Chem. 238, 3762-3769) inhibited Pi binding. The adenine nucleotides ADP, ATP, and the ATP analog adenylyl imidodiphosphate as well as the Pi analog arsenate, also inhibited Pi binding. The observations suggest that the Pi binding site was located in or near an adenine nucleotide binding site on the molecule. | Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase. Beef heart mitochondrial ATPase (F1) exhibited a single binding site for Pi. The interaction with Pi was reversible, partially dependent on the presence of divalent metal ions, and characterized by a dissociation constant at pH 7.5 of 80 micronM. A variety of substances known to influence oxidative phosphorylation or the activity of the soluble ATPase (F1) also influenced Pi binding by the enzyme. Thus aurovertin, an inhibitor of oxidative phosphorylation, which was bound tightly by F1 and inhibited ATPase activity, enhanced Pi binding via a 4-fold increase in the affinity of the enzyme for Pi (KD = 20 micronM) but did not alter binding stoichiometry. Anions such as SO4(2-), SO3(2-), chromate, and 2,4-dinitrophenolate, which stimulated ATPase activity of F1, also enhanced Pi binding. Inhibitors of ATPase activity such as nickel/bathophenanthroline and the protein ATPase inhibitor of Pullman and Monroy (Pullman, M. E., and Monroy, G. C. (1963) J. Biol. Chem. 238, 3762-3769) inhibited Pi binding. The adenine nucleotides ADP, ATP, and the ATP analog adenylyl imidodiphosphate as well as the Pi analog arsenate, also inhibited Pi binding. The observations suggest that the Pi binding site was located in or near an adenine nucleotide binding site on the molecule. | [
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PMID:16007 | Derepression of amino acid transport by amino acid starvation in rat hepatoma cells. | Amino acid starvation causes an adaptive increase in the initial rate of transport of selected neutral amino acids in an established line of rat hepatoma cells in tissue culture. After a lag of 30 min, the initial rate of transport of alpha-aminoisobutyric acid (AIB) increases to a maximum after 4 to 6 h starvation of 2 to 3 times that seen in control cells. The increased rate of transport is accompanied by an increase in the Vmax and a modest decrease in the Km for this transport system, and is reversed by readdition of amino acids. The enhancement is specific for amino acids transported by the A or alanine-preferring system (AIB, glycine, proline); uptake of amino acids transported by the L or leucine-preferring system (threonine, phenylalanine, tyrosine, leucine) or the Ly+ system for dibasci amino acids (lysine) is decreased under these conditions. Amino acids which compete with AIB for transport also prevent the starvation-induced increase in AIB transport; amino acids which do not compete fail to prevent the enhancement. Paradoxically threonine, phenylalanine, tryptophan, and tyrosine, which do not compete with AIB for transport, block the enhancement of transport upon amino acid starvation. The starvation-induced enhancement of amino acid transport does not appear to be the result of a release from transinhibition. After 30 min of amino acid starvation, AIB transport is either unchanged or slightly decreased even though amino acid pools are already depleted. Furthermore, loading cells with high concentrations of a single amino acid following a period of amino acid starvation fails to prevent the enhancement of AIB transport, whereas incubation of the cells with the single amino acid for the entire duration of amino acid starvation prevents the enhancement; intracellular amino acid pools are similar under both conditions. The enhancement of amino acid transport requires concomitant RNA and protein synthesis, consistent with the view that the adaptive increase reflects an increased amount of a rate-limiting protein involved in the transport process. Dexamethasone, which dramatically inhibits AIB transport in cells incubated in amino acid-containing medium, both blocks the starvation-induced increase in AIB transport, and causes a time-dependent decrease in transport velocity in cells whose transport has previously been enhanced by starvation. | Derepression of amino acid transport by amino acid starvation in rat hepatoma cells. Amino acid starvation causes an adaptive increase in the initial rate of transport of selected neutral amino acids in an established line of rat hepatoma cells in tissue culture. After a lag of 30 min, the initial rate of transport of alpha-aminoisobutyric acid (AIB) increases to a maximum after 4 to 6 h starvation of 2 to 3 times that seen in control cells. The increased rate of transport is accompanied by an increase in the Vmax and a modest decrease in the Km for this transport system, and is reversed by readdition of amino acids. The enhancement is specific for amino acids transported by the A or alanine-preferring system (AIB, glycine, proline); uptake of amino acids transported by the L or leucine-preferring system (threonine, phenylalanine, tyrosine, leucine) or the Ly+ system for dibasci amino acids (lysine) is decreased under these conditions. Amino acids which compete with AIB for transport also prevent the starvation-induced increase in AIB transport; amino acids which do not compete fail to prevent the enhancement. Paradoxically threonine, phenylalanine, tryptophan, and tyrosine, which do not compete with AIB for transport, block the enhancement of transport upon amino acid starvation. The starvation-induced enhancement of amino acid transport does not appear to be the result of a release from transinhibition. After 30 min of amino acid starvation, AIB transport is either unchanged or slightly decreased even though amino acid pools are already depleted. Furthermore, loading cells with high concentrations of a single amino acid following a period of amino acid starvation fails to prevent the enhancement of AIB transport, whereas incubation of the cells with the single amino acid for the entire duration of amino acid starvation prevents the enhancement; intracellular amino acid pools are similar under both conditions. The enhancement of amino acid transport requires concomitant RNA and protein synthesis, consistent with the view that the adaptive increase reflects an increased amount of a rate-limiting protein involved in the transport process. Dexamethasone, which dramatically inhibits AIB transport in cells incubated in amino acid-containing medium, both blocks the starvation-induced increase in AIB transport, and causes a time-dependent decrease in transport velocity in cells whose transport has previously been enhanced by starvation. | [
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PMID:16008 | Adrenodoxin reductase and adrenodoxin. Mechanisms of reduction of ferricyanide and cytochrome c. | Adrenodoxin reductase, the flavoprotein moiety of the adrenal cortex mitochondrial steroid hydroxylating system, participates in adrenodoxin-dependent cytochrome c and adrenodoxin-independent ferricyanide reduction, with NADPH as electron donor for both of these 1-electron reductions. For ferricyanide reduction, adrenodoxin reductase cycles between oxidized and 2-electron-reduced forms, reoxidation proceeding via the neutral flavin (FAD) semiquinone form (Fig. 9). Addition of adrenodoxin has no effect upon the kinetic parameters of flavoprotein-catalyzed ferricyanide reduction. For cytochrome c reduction, the adrenodoxin reductase-adrenodoxin 1:1 complex has been shown to be the catalytically active species (Lambeth, J. D., McCaslin, D. R., and Kamin, H. (1976) J. Biol. Chem. 251, 7545-7550). Present studies, using stopped flow techniques, have shown that the 2-electron-reduced form of the complex (produced by reaction with 1 eq of NADPH) reacts rapidly with 1 eq of cytochrome c (k approximately or equal to 4.6 s-1), but only slowly with a second cytochrome c (k = 0.1 to 0.3 s-1). However, when a second NADPH is included, two more equivalents of cytochrome are reduced rapidly. Thus, the adrenodoxin reductase-adrenodoxin complex appears to cycle between 1- and 3-electron reduced states, via an intermediate 2-electron-containing form produced by reoxidation by cytochrome (Fig. 10). For ferricyanide reduction by adrenodoxin reductase, the fully reduced and semiquinone forms of flavin each transfer 1 electron at oxidation-reduction potentials which differ by approximately 130 mV. However, adrenodoxin in a complex with adrenodoxin reductase allows electrons of constant potential to be delivered from flavin to cytochrome c via the iron sulfur center... | Adrenodoxin reductase and adrenodoxin. Mechanisms of reduction of ferricyanide and cytochrome c. Adrenodoxin reductase, the flavoprotein moiety of the adrenal cortex mitochondrial steroid hydroxylating system, participates in adrenodoxin-dependent cytochrome c and adrenodoxin-independent ferricyanide reduction, with NADPH as electron donor for both of these 1-electron reductions. For ferricyanide reduction, adrenodoxin reductase cycles between oxidized and 2-electron-reduced forms, reoxidation proceeding via the neutral flavin (FAD) semiquinone form (Fig. 9). Addition of adrenodoxin has no effect upon the kinetic parameters of flavoprotein-catalyzed ferricyanide reduction. For cytochrome c reduction, the adrenodoxin reductase-adrenodoxin 1:1 complex has been shown to be the catalytically active species (Lambeth, J. D., McCaslin, D. R., and Kamin, H. (1976) J. Biol. Chem. 251, 7545-7550). Present studies, using stopped flow techniques, have shown that the 2-electron-reduced form of the complex (produced by reaction with 1 eq of NADPH) reacts rapidly with 1 eq of cytochrome c (k approximately or equal to 4.6 s-1), but only slowly with a second cytochrome c (k = 0.1 to 0.3 s-1). However, when a second NADPH is included, two more equivalents of cytochrome are reduced rapidly. Thus, the adrenodoxin reductase-adrenodoxin complex appears to cycle between 1- and 3-electron reduced states, via an intermediate 2-electron-containing form produced by reoxidation by cytochrome (Fig. 10). For ferricyanide reduction by adrenodoxin reductase, the fully reduced and semiquinone forms of flavin each transfer 1 electron at oxidation-reduction potentials which differ by approximately 130 mV. However, adrenodoxin in a complex with adrenodoxin reductase allows electrons of constant potential to be delivered from flavin to cytochrome c via the iron sulfur center... | [
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PMID:16009 | Alpha-ketoglutarate dehydrogenase complex of Acetobacter xylinum. Purification and regulatory properties. | The alpha-ketoglutarate dehydrogenase complex of Acetobacter xylinum was purified to homogeneity. It consists of three main polypeptide chains with a total molecular weight of about 2.4 X 10(6). It catalyzes the overall Mg2+ and thiamin pyrophosphate-dependent, NAD+- and CoA-linked oxidative decarboxylation of alpha-ketoglutarate, as well as the partial reactions characteristic of the three enzyme components described for the complex from other sources. Initial velocity studies revealed marked positive cooperativity for the substrate alpha-ketoglutarate (Hill coefficient (nH) = 2.0; concentration of ligand at half-maximum effect (S0.5) = 8 mM). The sigmoidal [alpha-ketoglutarate]-velocity relationship became hyperbolic upon addition of AMP or 3-acetylpyridine adenine dinucleotide (AcPyAD) or in the presence of high concentrations of NAD. S0.5 (alpha-ketoglutarate) decreased to 1 mM, but Vmax was unchanged. Saturation curves for NAD and AMP are sigmoidal (nH = 2) at low alpha-ketoglutarate concentrations and become hyperbolic at high alpha-ketoglutarate concentrations. As judged by S0.5, the relative efficiency of the allosteric effectors is AcPyAD greater than AMP greater than alpha-ketoglutarate- greater than NAD+. Half-maximal changes in nH, S0.5, and activation by AMP occur at a pH significantly different from that of half-maximal activity. A model for the allosteric behavior of the complex is proposed in which the first enzyme component of the complex (E1) is the site for the allosteric interactions and AMP is the primary positive modifier, whereas NAD and AcPyAD act as AMP analogues. The overall reaction is competitively inhibited by NADH with respect to NAD (K1 = 20 micronM) and by succinyl-CoA with respect of CoA (K1 = 3 micronM). The properties of the alpha-ketoglutarate dehydrogenase complex of A. xylinum appear to provide for appropriate partitioning of alpha-ketoglutarate carbon between competing pathways in response to the energy state of the cells. | Alpha-ketoglutarate dehydrogenase complex of Acetobacter xylinum. Purification and regulatory properties. The alpha-ketoglutarate dehydrogenase complex of Acetobacter xylinum was purified to homogeneity. It consists of three main polypeptide chains with a total molecular weight of about 2.4 X 10(6). It catalyzes the overall Mg2+ and thiamin pyrophosphate-dependent, NAD+- and CoA-linked oxidative decarboxylation of alpha-ketoglutarate, as well as the partial reactions characteristic of the three enzyme components described for the complex from other sources. Initial velocity studies revealed marked positive cooperativity for the substrate alpha-ketoglutarate (Hill coefficient (nH) = 2.0; concentration of ligand at half-maximum effect (S0.5) = 8 mM). The sigmoidal [alpha-ketoglutarate]-velocity relationship became hyperbolic upon addition of AMP or 3-acetylpyridine adenine dinucleotide (AcPyAD) or in the presence of high concentrations of NAD. S0.5 (alpha-ketoglutarate) decreased to 1 mM, but Vmax was unchanged. Saturation curves for NAD and AMP are sigmoidal (nH = 2) at low alpha-ketoglutarate concentrations and become hyperbolic at high alpha-ketoglutarate concentrations. As judged by S0.5, the relative efficiency of the allosteric effectors is AcPyAD greater than AMP greater than alpha-ketoglutarate- greater than NAD+. Half-maximal changes in nH, S0.5, and activation by AMP occur at a pH significantly different from that of half-maximal activity. A model for the allosteric behavior of the complex is proposed in which the first enzyme component of the complex (E1) is the site for the allosteric interactions and AMP is the primary positive modifier, whereas NAD and AcPyAD act as AMP analogues. The overall reaction is competitively inhibited by NADH with respect to NAD (K1 = 20 micronM) and by succinyl-CoA with respect of CoA (K1 = 3 micronM). The properties of the alpha-ketoglutarate dehydrogenase complex of A. xylinum appear to provide for appropriate partitioning of alpha-ketoglutarate carbon between competing pathways in response to the energy state of the cells. | [
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|
PMID:16010 | Oxygen-linked CO2 binding to isolated beta subunits of human hemoglobin. | It is known that most of the oxygen-linked carbamate which is formed in normal adult human hemoglobin (Hb A) is confined to the beta subunits rather than to the alpha subunits. In order to find out if similar differences exist in the isolated protomers of Hb A we have measured the effect of various pressures of carbon dioxide (pCO2) on the oxygen affinity in the following heme pigments: isolated alpha and beta subunits with free --SH groups (alphaSH, betaSH), mercurated beta subunits (betaPMB), myoglobin (Mb), and betaSH/PLP in which the terminal alpha-amino group of betaSH was irreversibly blocked with pyridoxal phosphate (PLP). Similar measurements were done on Hb A and the fraction of oxygen-linked carbamate calculated from the effect of pCO2 (at constant pH) on the oxygen half-saturation pressure (p50). A distinct influence of CO2 on p50 was observed in betaSH which was absent in betaSH/PLP and thus indicates that the terminal alpha-amino group mediates the oxygen-linked binding of CO2 in betaSH as it does in the beta subunits of Hb A. However, the fraction of oxygen-linked carbamate was much less dependent on pH and pCO2 in betaSH than in Hb A. Neither alphaSH, betaPMB, or Mb, all of which are known to exist largely or wholly as monomers but have free terminal alpha-amino groups, showed a shift of p50 upon addition of CO2. As both betaSH and betaSH/PLP were shown to be tetrameric molecules, we conclude from this study that homotetramers composed of isolated beta subunits do exhibit a reciprocal interaction between the binding of O2 and CO2. | Oxygen-linked CO2 binding to isolated beta subunits of human hemoglobin. It is known that most of the oxygen-linked carbamate which is formed in normal adult human hemoglobin (Hb A) is confined to the beta subunits rather than to the alpha subunits. In order to find out if similar differences exist in the isolated protomers of Hb A we have measured the effect of various pressures of carbon dioxide (pCO2) on the oxygen affinity in the following heme pigments: isolated alpha and beta subunits with free --SH groups (alphaSH, betaSH), mercurated beta subunits (betaPMB), myoglobin (Mb), and betaSH/PLP in which the terminal alpha-amino group of betaSH was irreversibly blocked with pyridoxal phosphate (PLP). Similar measurements were done on Hb A and the fraction of oxygen-linked carbamate calculated from the effect of pCO2 (at constant pH) on the oxygen half-saturation pressure (p50). A distinct influence of CO2 on p50 was observed in betaSH which was absent in betaSH/PLP and thus indicates that the terminal alpha-amino group mediates the oxygen-linked binding of CO2 in betaSH as it does in the beta subunits of Hb A. However, the fraction of oxygen-linked carbamate was much less dependent on pH and pCO2 in betaSH than in Hb A. Neither alphaSH, betaPMB, or Mb, all of which are known to exist largely or wholly as monomers but have free terminal alpha-amino groups, showed a shift of p50 upon addition of CO2. As both betaSH and betaSH/PLP were shown to be tetrameric molecules, we conclude from this study that homotetramers composed of isolated beta subunits do exhibit a reciprocal interaction between the binding of O2 and CO2. | [
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|
PMID:16011 | Adenosine triphosphate synthesis by electrochemical proton gradient in vesicles reconstituted from purified adenosine triphosphatase and phospholipids of thermophilic bacterium. | Vesicles were reconstituted from a purified dicyclohexyl-carbodiimide-sensitive ATPase complex (TF0-F1) and phospholipids of a thermophilic bacterium PS3. These vesicles synthesized ATP from ADP and Pi with energy from an electrochemical proton gradient (delta-micronH+) formed by a pH gradient and an electrical potential across their membranes. Maximal ATP synthesis was achieved by incubating the vesicles in malonate at pH 5.5 with valinomycin, and then rapidly transferring them to a solution of pH 8.4 and 150 mM K+. Under these conditons ATP synthesis continued at a decreasing rate for 30 s at 40 degrees. Appreciable formation of ATP (40 to 150 nmol/mg of TF0-F1) occurred at an initial delta-micronH+ above 205 mV and moderate formation at an initial value above 180 mV. ATP hydrolysis by the vesicles produced a delta-micronH+, and the additions of 32Pi and hexokinase to them resulted in 32Pi esterification. Analysis of the time courses of 32Pi esterification and decays of the pH difference and membrane potential, followed using 9-aminoacridine and 8-anilinonaphthalene-1-sulfonate, respectively, as probes, showed a relationship between delta-micronH+ and the rate of ATP synthesis. These results demonstrate that purified TF0-F1 is itself a reversible H+-translocating ATPase of oxidative phosphorylation. | Adenosine triphosphate synthesis by electrochemical proton gradient in vesicles reconstituted from purified adenosine triphosphatase and phospholipids of thermophilic bacterium. Vesicles were reconstituted from a purified dicyclohexyl-carbodiimide-sensitive ATPase complex (TF0-F1) and phospholipids of a thermophilic bacterium PS3. These vesicles synthesized ATP from ADP and Pi with energy from an electrochemical proton gradient (delta-micronH+) formed by a pH gradient and an electrical potential across their membranes. Maximal ATP synthesis was achieved by incubating the vesicles in malonate at pH 5.5 with valinomycin, and then rapidly transferring them to a solution of pH 8.4 and 150 mM K+. Under these conditons ATP synthesis continued at a decreasing rate for 30 s at 40 degrees. Appreciable formation of ATP (40 to 150 nmol/mg of TF0-F1) occurred at an initial delta-micronH+ above 205 mV and moderate formation at an initial value above 180 mV. ATP hydrolysis by the vesicles produced a delta-micronH+, and the additions of 32Pi and hexokinase to them resulted in 32Pi esterification. Analysis of the time courses of 32Pi esterification and decays of the pH difference and membrane potential, followed using 9-aminoacridine and 8-anilinonaphthalene-1-sulfonate, respectively, as probes, showed a relationship between delta-micronH+ and the rate of ATP synthesis. These results demonstrate that purified TF0-F1 is itself a reversible H+-translocating ATPase of oxidative phosphorylation. | [
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|
PMID:16012 | Pure Renin. Isolation from hog kidney and characterization. | The pressor enzyme renin (EC 3.4.99.19) was isolated in a pure and stable form from hog kidney by affinity chromatography on a pepstatin/agarose gel followed by three additional steps of conventional chromatography. Destruction of the enzyme by proteolysis during isolation was prevented by chemically eliminating proteases in extracts. The pure preparation was used for the characterization of this enzyme. Renin was found to be a glycoprotein containing glucosamine and possessing binding affinity to concanavalin A. Contrary to previous reports, pure renin is stable at neutral pH either at 4 or -20 degrees for 3 to 8 weeks. It has a molecular weight of 36,400 as determined by equilibrium ultracentrifugation, an isoelectric point of 5.2 and E1%1cm (280 nm) of 9.1. In contrast to crude preparations, the enzyme activity has a broad pH optimum between pH 5.5 and 7.0 for both hog angiotensinogen and the synthetic octapeptide substrate benzyloxycarbonyl-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser-beta-naphthylamide. The rate of formation of angiotensin I from hog angiotensinogen at pH 6.0 and 37 degrees was 267 microng/h/microng of renin, or 2000 Goldblatt units/mg of renin. For the synthetic fluorogenic octapeptide substrate benzyloxycarbonyl-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser-beta-naphthylamide, a Km of 33 micronM and a Vmax of 0.94 micronmol/h/mg of enzyme were obtained at pH 6.5 and 37 degrees. | Pure Renin. Isolation from hog kidney and characterization. The pressor enzyme renin (EC 3.4.99.19) was isolated in a pure and stable form from hog kidney by affinity chromatography on a pepstatin/agarose gel followed by three additional steps of conventional chromatography. Destruction of the enzyme by proteolysis during isolation was prevented by chemically eliminating proteases in extracts. The pure preparation was used for the characterization of this enzyme. Renin was found to be a glycoprotein containing glucosamine and possessing binding affinity to concanavalin A. Contrary to previous reports, pure renin is stable at neutral pH either at 4 or -20 degrees for 3 to 8 weeks. It has a molecular weight of 36,400 as determined by equilibrium ultracentrifugation, an isoelectric point of 5.2 and E1%1cm (280 nm) of 9.1. In contrast to crude preparations, the enzyme activity has a broad pH optimum between pH 5.5 and 7.0 for both hog angiotensinogen and the synthetic octapeptide substrate benzyloxycarbonyl-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser-beta-naphthylamide. The rate of formation of angiotensin I from hog angiotensinogen at pH 6.0 and 37 degrees was 267 microng/h/microng of renin, or 2000 Goldblatt units/mg of renin. For the synthetic fluorogenic octapeptide substrate benzyloxycarbonyl-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser-beta-naphthylamide, a Km of 33 micronM and a Vmax of 0.94 micronmol/h/mg of enzyme were obtained at pH 6.5 and 37 degrees. | [
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|
PMID:16013 | Neurospora crassa glutamine synthetase. Translation of specific messenger ribonucleic acid in a cell-free system derived from rabbit reticulocytes. | The total reticulocyte lysate cell-free protein-synthesizing system was incubated in the presence of Neurospora crassa RNA. With the aid of an antibody directed against purified N. crassa glutamine synthetase, the synthesis of a specific protein was detected. This protein precipitates with antiglutamine synthetase using both direct and indirect procedures, migrates with the same molecular weight as the monomer of N. crassa glutamine synthetase when subjected to acrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, and chromatographs as N. crassa glutamine synthetase on anthranilate-bound Sepharose. These data indicate the translation of the mRNA that codes for N. crassa glutamine synthetase. This RNA behaves as poly(A)-containing material when fractionated on oly(U)-Sepha-rose. | Neurospora crassa glutamine synthetase. Translation of specific messenger ribonucleic acid in a cell-free system derived from rabbit reticulocytes. The total reticulocyte lysate cell-free protein-synthesizing system was incubated in the presence of Neurospora crassa RNA. With the aid of an antibody directed against purified N. crassa glutamine synthetase, the synthesis of a specific protein was detected. This protein precipitates with antiglutamine synthetase using both direct and indirect procedures, migrates with the same molecular weight as the monomer of N. crassa glutamine synthetase when subjected to acrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, and chromatographs as N. crassa glutamine synthetase on anthranilate-bound Sepharose. These data indicate the translation of the mRNA that codes for N. crassa glutamine synthetase. This RNA behaves as poly(A)-containing material when fractionated on oly(U)-Sepha-rose. | [
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|
PMID:16014 | Solubilization and properties of mannose and N-acetylglucosamine transferases involved in formation of polyprenyl-sugar intermediates. | A particulate fraction from porcine aorta catalyzed the incorporation of N-acetylglucosamine (GlcNAc) from UDP-[3H]GlcNAc into both GlcNAc-pyrophosphorylpolyprenol and GlcNAc-GlcNAc-pyrophosphorylpolyprenol. This transfer utilized endogenous lipid and required a divalent cation. Mn2+ was the best metal ion and was optimum at 2.3 mM. This same particulate fraction was previously shown to transfer mannose from GDP-[14C]mannose to endogenous lipid to form mannosylphosphorylpolyprenol (Chambers, J., and Elbein, A.D. (1975) J. Biol. Chem. 250, 6904-6915). Both the GlcNAc activities and the mannose activity were solubilized by treatment of the particulate fraction with the detergent Nonidet P-40. The enzymes were partially purified by chromatography on DEAE-cellulose and on Sephadex G-200. These soluble enzymes required the addition of acceptor lipid for activity. An acidic lipid fraction, isolated from pig liver and having the properties of dolichyl phosphate, was active with either the GlcNAc or the mannose transferase. Chemically synthesized dolichyl phosphate was also active with either of these enzymes. The products formed from either GlcNAc or mannose by the soluble transferases were similar to those formed by the particulate enzyme. Thus the major product formed from UDP-[3H]GlcNAc was GlcNAc-pyrophosphoryldolichol with small amounts of the disaccharide-lipid while the product formed from GDP-[14C]mannose was mannosylphosphoryldolichol. | Solubilization and properties of mannose and N-acetylglucosamine transferases involved in formation of polyprenyl-sugar intermediates. A particulate fraction from porcine aorta catalyzed the incorporation of N-acetylglucosamine (GlcNAc) from UDP-[3H]GlcNAc into both GlcNAc-pyrophosphorylpolyprenol and GlcNAc-GlcNAc-pyrophosphorylpolyprenol. This transfer utilized endogenous lipid and required a divalent cation. Mn2+ was the best metal ion and was optimum at 2.3 mM. This same particulate fraction was previously shown to transfer mannose from GDP-[14C]mannose to endogenous lipid to form mannosylphosphorylpolyprenol (Chambers, J., and Elbein, A.D. (1975) J. Biol. Chem. 250, 6904-6915). Both the GlcNAc activities and the mannose activity were solubilized by treatment of the particulate fraction with the detergent Nonidet P-40. The enzymes were partially purified by chromatography on DEAE-cellulose and on Sephadex G-200. These soluble enzymes required the addition of acceptor lipid for activity. An acidic lipid fraction, isolated from pig liver and having the properties of dolichyl phosphate, was active with either the GlcNAc or the mannose transferase. Chemically synthesized dolichyl phosphate was also active with either of these enzymes. The products formed from either GlcNAc or mannose by the soluble transferases were similar to those formed by the particulate enzyme. Thus the major product formed from UDP-[3H]GlcNAc was GlcNAc-pyrophosphoryldolichol with small amounts of the disaccharide-lipid while the product formed from GDP-[14C]mannose was mannosylphosphoryldolichol. | [
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|
PMID:16015 | Effects of caffeine and other methylxanthines on the development and metabolism of sea urchin eggs. Involvement of NADP and glutathione. | Methylxanthines (MX) inhibit cell division in sea urchin and clam eggs. This inhibitory effect is not mediated via cAMP. MX also inhibit respiration in marine eggs, at concentrations which inhibit cleavage. Studies showed that no changes occurred in ATP and ADP levels in the presence of inhibitory concentrations of MX, indicating an extra-mitochondrial site of action for the drug. Subsequent studies revealed decreased levels of NADP+ and NADPH, when eggs were incubated with inhibitory concentrations of MX, but no change in levels of NAD+ and NADH. MX did not affect the pentose phosphate shunt pathway and did not have any effect on the enzyme NAD+ -kinase. Further studies showed a marked inhibitory effect on the glutathione reductase activity of MX-treated eggs. Reduced glutathione (GSH) could reverse the cleavage inhibitory effect of MX. Moreover, diamide, a thiol-oxidizing agent specific for GSH in living cells, caused inhibition of cell division in sea urchin eggs. Diamide added to eggs containing mitotic apparatus (MA) could prevent cleavage by causing a dissolution of the formed MA. Both MX and diamide inhibit a Ca2+-activated ATPase in whole eggs. The enzyme can be reactivated by sulfhydryl reducing agents added in the assay mixture. In addition, diamide causes an inhibition of microtubule polymerization, reversible with dithioerythritol. All experimental evidence so far suggests that inhibition of mitosis in sea urchin eggs by MX is mediated by perturbations of the in vivo thiol-disulfide status of target systems, with a primary effect on glutathione levels. | Effects of caffeine and other methylxanthines on the development and metabolism of sea urchin eggs. Involvement of NADP and glutathione. Methylxanthines (MX) inhibit cell division in sea urchin and clam eggs. This inhibitory effect is not mediated via cAMP. MX also inhibit respiration in marine eggs, at concentrations which inhibit cleavage. Studies showed that no changes occurred in ATP and ADP levels in the presence of inhibitory concentrations of MX, indicating an extra-mitochondrial site of action for the drug. Subsequent studies revealed decreased levels of NADP+ and NADPH, when eggs were incubated with inhibitory concentrations of MX, but no change in levels of NAD+ and NADH. MX did not affect the pentose phosphate shunt pathway and did not have any effect on the enzyme NAD+ -kinase. Further studies showed a marked inhibitory effect on the glutathione reductase activity of MX-treated eggs. Reduced glutathione (GSH) could reverse the cleavage inhibitory effect of MX. Moreover, diamide, a thiol-oxidizing agent specific for GSH in living cells, caused inhibition of cell division in sea urchin eggs. Diamide added to eggs containing mitotic apparatus (MA) could prevent cleavage by causing a dissolution of the formed MA. Both MX and diamide inhibit a Ca2+-activated ATPase in whole eggs. The enzyme can be reactivated by sulfhydryl reducing agents added in the assay mixture. In addition, diamide causes an inhibition of microtubule polymerization, reversible with dithioerythritol. All experimental evidence so far suggests that inhibition of mitosis in sea urchin eggs by MX is mediated by perturbations of the in vivo thiol-disulfide status of target systems, with a primary effect on glutathione levels. | [
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|
PMID:16016 | Quantitative studies on the polarization optical properties of striated muscle. I. Birefringence changes of rabbit psoas muscle in the transition from rigor to relaxed state. | The changes in birefringence in the rigor to relax transition of single triton-extracted rabbit psoas muscle fibers have been investigated with quantitative polarized light techniques. The total birefringence of rest lenght fibers in rigor was (1.46 +/- 0.08) x 10(-3) and increased to (1.67 +/- 0.05) x 10(-3) after Mg-ATP relaxation. Pyrophosphate relaxation increased the total birefringence only slightly, whereas subsequent Mg-ATP relaxation elicited the maximum increase in birefringence. Changes in lattice spacing did not account for the total increase in birefrigence during relaxation. Moreover, the increase in total birefringence was attributable to increases in intrinsic birefringence as well as form birefringence. No change in birefringence was exhibited upon exposure to a relaxation solution after myosin extraction. Synthetic myosin filaments were prepared and treated with relaxation and rigor solutions. The negatively stained filaments treated with a rigor solution had gross irregular projections at either end, while the filaments treated with a relaxing solution were more spindle shaped. The results are compatible with the view that the subfragment-2 moieties of myosin angle away from the myosin aggregates (light meromyosin) to permit the attachment of the subfragment-1 moieties to actin. | Quantitative studies on the polarization optical properties of striated muscle. I. Birefringence changes of rabbit psoas muscle in the transition from rigor to relaxed state. The changes in birefringence in the rigor to relax transition of single triton-extracted rabbit psoas muscle fibers have been investigated with quantitative polarized light techniques. The total birefringence of rest lenght fibers in rigor was (1.46 +/- 0.08) x 10(-3) and increased to (1.67 +/- 0.05) x 10(-3) after Mg-ATP relaxation. Pyrophosphate relaxation increased the total birefringence only slightly, whereas subsequent Mg-ATP relaxation elicited the maximum increase in birefringence. Changes in lattice spacing did not account for the total increase in birefrigence during relaxation. Moreover, the increase in total birefringence was attributable to increases in intrinsic birefringence as well as form birefringence. No change in birefringence was exhibited upon exposure to a relaxation solution after myosin extraction. Synthetic myosin filaments were prepared and treated with relaxation and rigor solutions. The negatively stained filaments treated with a rigor solution had gross irregular projections at either end, while the filaments treated with a relaxing solution were more spindle shaped. The results are compatible with the view that the subfragment-2 moieties of myosin angle away from the myosin aggregates (light meromyosin) to permit the attachment of the subfragment-1 moieties to actin. | [
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PMID:16017 | Different sensitivity of DNA in situ in interphase and metaphase chromatin to heat denaturation. | Heat denaturation of DNA in situ, in unbroken cells, was studied in relation to the cell cycle. DNA in metaphase cells denatured at lower temperatures (8 degrees-10 degrees C lower) than DNA in interphase cells. Among interphase cells, small differences between G1, S, and G2 cells were observed at temperatures above 90 degrees C. The difference between metaphase and interphase cells increased after short pretreatment with formaldehyde, decreased when cells were heated in the presence of 1 mM MgCl2, and was abolished by cell pretreatment with 0.5 N HCl. The results suggest that acid-soluble constituents of chromatin confer local stability to DNA and that the degree of stabilization is lower in metaphase chromosomes than in interphase nuclei. These in situ results remain in contrast to the published data showing no difference in DNA denaturation in chromatin isolated from interphase and metaphase cells. It is likely that factors exist which influence the stability of DNA in situ are associated with the super-structural organization of chromatin in intact nuclei and which are lost during chromatin isolation and solubilization. Since DNA denaturation is assayed after cell cooling, there is also a possibility that the extent of denatured DNA may be influenced by some factors that control strand separation and DNA reassociation. The different stainability of interphase vs. metaphase cells, based on the difference in stability of DNA, offers a method for determining mitotic indices by flow cytofluorometry, and a possible new parameter for sorting cells in metaphase. | Different sensitivity of DNA in situ in interphase and metaphase chromatin to heat denaturation. Heat denaturation of DNA in situ, in unbroken cells, was studied in relation to the cell cycle. DNA in metaphase cells denatured at lower temperatures (8 degrees-10 degrees C lower) than DNA in interphase cells. Among interphase cells, small differences between G1, S, and G2 cells were observed at temperatures above 90 degrees C. The difference between metaphase and interphase cells increased after short pretreatment with formaldehyde, decreased when cells were heated in the presence of 1 mM MgCl2, and was abolished by cell pretreatment with 0.5 N HCl. The results suggest that acid-soluble constituents of chromatin confer local stability to DNA and that the degree of stabilization is lower in metaphase chromosomes than in interphase nuclei. These in situ results remain in contrast to the published data showing no difference in DNA denaturation in chromatin isolated from interphase and metaphase cells. It is likely that factors exist which influence the stability of DNA in situ are associated with the super-structural organization of chromatin in intact nuclei and which are lost during chromatin isolation and solubilization. Since DNA denaturation is assayed after cell cooling, there is also a possibility that the extent of denatured DNA may be influenced by some factors that control strand separation and DNA reassociation. The different stainability of interphase vs. metaphase cells, based on the difference in stability of DNA, offers a method for determining mitotic indices by flow cytofluorometry, and a possible new parameter for sorting cells in metaphase. | [
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PMID:16018 | Submitochondrial localization and function of enzymes of glutamine metabolism in avian liver. | Glutamine synthetase (EC 6.3.1.2) was localized within the matrix compartment of avian liver mitochondria. The submitochondrial localization of this enzyme was determined by the digitonin-Lubrol method of Schnaitman and Greenawalt (35). The matrix fraction contained over 74% of the glutamine synthetase activity and the major proportion of the matirx marker enzymes, malate dehydrogenase (71%), NADP-dependent isocitrate dehydrogenase (83%), and glutamate dehydrogenase (57%). The highest specific activities of these enzymes were also found in the matrix compartment. Oxidation of glutamine by avian liver mitochondria was substantially less than that of glutamate. Bromofuroate, an inhibitor of glutamate dehydrogenase, blocked oxidation of glutamate and of glutamine whereas aminoxyacetate, a transaminase inhibitor, had little or no effect with either substrate. These results indicate that glutamine metabolism is probably initiated by the conversion of glutamine to glutamate rather than to an alpha-keto acid. The localization of a glutaminase activity within avian liver mitochondria plus the absence of an active mitochondrial glutamine transaminase is consistent with the differential effects of the transaminase and glutamate dehydrogenase inhibitors. The high glutamine synthetase activity (40:1) suggests that mitochondrial catabolism of glutamine is minimal, freeing most of the glutamine synthesized for purine (uric acid) biosynthesis. | Submitochondrial localization and function of enzymes of glutamine metabolism in avian liver. Glutamine synthetase (EC 6.3.1.2) was localized within the matrix compartment of avian liver mitochondria. The submitochondrial localization of this enzyme was determined by the digitonin-Lubrol method of Schnaitman and Greenawalt (35). The matrix fraction contained over 74% of the glutamine synthetase activity and the major proportion of the matirx marker enzymes, malate dehydrogenase (71%), NADP-dependent isocitrate dehydrogenase (83%), and glutamate dehydrogenase (57%). The highest specific activities of these enzymes were also found in the matrix compartment. Oxidation of glutamine by avian liver mitochondria was substantially less than that of glutamate. Bromofuroate, an inhibitor of glutamate dehydrogenase, blocked oxidation of glutamate and of glutamine whereas aminoxyacetate, a transaminase inhibitor, had little or no effect with either substrate. These results indicate that glutamine metabolism is probably initiated by the conversion of glutamine to glutamate rather than to an alpha-keto acid. The localization of a glutaminase activity within avian liver mitochondria plus the absence of an active mitochondrial glutamine transaminase is consistent with the differential effects of the transaminase and glutamate dehydrogenase inhibitors. The high glutamine synthetase activity (40:1) suggests that mitochondrial catabolism of glutamine is minimal, freeing most of the glutamine synthesized for purine (uric acid) biosynthesis. | [
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PMID:16019 | The influence of culture conditions on the induction of tyrosine aminotransferase by cyclic nucleotides in rat hepatoma cells. | The increase in tyrosine aminotransferase activity which occurs in rat hepatoma tissue culture (HTC) cells in response to cyclic AMP analogs has been shown to be an enzyme induction, similar to the larger response observed in certain other hepatoma cells and in liver. A specific antibody to tyrosine aminotransferase has been used to show that the number of enzyme molecules and the rate of enzyme synthesis are increased by N6,O2'-dibutyryl cyclic AMP in HTC cells. The effect on tyrosine aminotransferase is also produced by various 8-substituted derivatives of cyclic AMP and occurs whether or not the enzyme has been preinduced with a glucocorticoid. The response of the enzyme is greater when HTC cells are maintained in monolayer than in suspension cultures. Neither cell growth nor serum is required for the response. | The influence of culture conditions on the induction of tyrosine aminotransferase by cyclic nucleotides in rat hepatoma cells. The increase in tyrosine aminotransferase activity which occurs in rat hepatoma tissue culture (HTC) cells in response to cyclic AMP analogs has been shown to be an enzyme induction, similar to the larger response observed in certain other hepatoma cells and in liver. A specific antibody to tyrosine aminotransferase has been used to show that the number of enzyme molecules and the rate of enzyme synthesis are increased by N6,O2'-dibutyryl cyclic AMP in HTC cells. The effect on tyrosine aminotransferase is also produced by various 8-substituted derivatives of cyclic AMP and occurs whether or not the enzyme has been preinduced with a glucocorticoid. The response of the enzyme is greater when HTC cells are maintained in monolayer than in suspension cultures. Neither cell growth nor serum is required for the response. | [
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|
PMID:16020 | The effect of medium pH on rate of growth, neurite formation and acetylcholinesterase activity in mouse neuroblastoma cells in culture. | Cell division, neurite formation and acetylcholinesterase activity were examined in a clone (NBA2) of mouse neuroblastoma cells maintained for up to 120 hours in medium with pH values between 6.6 and 8.0. Growth rate decreased as pH was reduced from 7.8 to 6.6. Generation time at pH 7.4 was 25 hours, while the rate of cell division was negligible at pH 6.6. The total number of cells at stationary phase was less at the lower pH values. Neurite formation was enhanced markedly as the pH was reduced from 7.4 to 6.6. Acetylcholinesterase activity was 5- to 8-fold greater in cells exposed to medium at pH 6.6 than in cells maintained in medium at pH 7.4. The reduction in the rate of cell division and increases in neurite formation and acetylcholinesterase activity at pH 6.6 were reversible upon exposure of the cells to pH 7.4 medium. Cell viability was greater than 90% at all medium pH values over a period of 120 hours. Uncloned T-59 mouse neuroblastoma cells were affected similarly by changes in pH. These results show that manipulation of the environmental pH can reversibly alter growth, neurite formation, and acetylcholinesterase activity of mouse neuroblastoma cells in culture. | The effect of medium pH on rate of growth, neurite formation and acetylcholinesterase activity in mouse neuroblastoma cells in culture. Cell division, neurite formation and acetylcholinesterase activity were examined in a clone (NBA2) of mouse neuroblastoma cells maintained for up to 120 hours in medium with pH values between 6.6 and 8.0. Growth rate decreased as pH was reduced from 7.8 to 6.6. Generation time at pH 7.4 was 25 hours, while the rate of cell division was negligible at pH 6.6. The total number of cells at stationary phase was less at the lower pH values. Neurite formation was enhanced markedly as the pH was reduced from 7.4 to 6.6. Acetylcholinesterase activity was 5- to 8-fold greater in cells exposed to medium at pH 6.6 than in cells maintained in medium at pH 7.4. The reduction in the rate of cell division and increases in neurite formation and acetylcholinesterase activity at pH 6.6 were reversible upon exposure of the cells to pH 7.4 medium. Cell viability was greater than 90% at all medium pH values over a period of 120 hours. Uncloned T-59 mouse neuroblastoma cells were affected similarly by changes in pH. These results show that manipulation of the environmental pH can reversibly alter growth, neurite formation, and acetylcholinesterase activity of mouse neuroblastoma cells in culture. | [
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|
PMID:16023 | Derivatization and chromatography of nucleosides and nucleotides. | The aims of this study were to determine the effect of levels of various substances and reaction by-products, which are formed during hydrolysis of nucleic acids, on the derivatization and chromatography of nucleosides; and to investigate the silylation of mono- and dinucleotides. The effect of NaCl, KCl, MgCl2, NH4Cl, and (NH4)2SO4 on silylation and chromatography of nucleosides was studies at various molar excesses of salt. The response values for all nucleosides were studied at various molar excesses of salt. The response values for all nucleosides were significantly affected at molar excess salt present values (MSP) between 1 and 10 for KCl, NaCl, NH4Cl, (NH4)2SO4 and between 0.1 and 1 for MgCl2. It was noted that thymidine was more sensitive than other nucleosides if silylated in presence of these salts. Two chromatographic peaks at retention temperatures (RT) 240 and 251 were obtained for cytidine at MSP values of 10(-3) for NaCl, KCl, and MgCl2, and 10(-4) for NH4Cl and (NH4)2SO4. In a mixture of nucleosides the RT = 251 peak was used for quantitative analysis of cytidine as the RT = 240 peak elutes with guanosine. Thus, these salts have a significant effect on the gas-liquid chromatography of trimethylsilyl (TMS) cytidine in a mixture of nucleosides, especially the RT = 241 peak. The effect of salts on derivatization can be explained in part as follows: (a) reduced derivatization of nucleosides due to a decreased solubility in the solvent system; (b) formation of TMS anion derivatives, e.g. TMS-SO4, TMS-PO4, with a reduced molar excess of BSTFA; (c) metal chelation by Mg ions or other divalent cations with nucleosides or BSTFA; and/or (d) an increased breakdown of TMS derivatives in presence of salt in the sample or on the top 3 in. of the column packing. Also, experiments were made on the effect of other substances such as Tris, phosphate, alkaline phosphatase, and KCl on completeness of silylation. The individual impurities showed no significant effect on the relative weight response (RWR) values of nucleosides; however, when a mixture was used, significantly lower RWR values were observed for all nucleosides except thymidine when using 1000 molar excess of BSTFA greater than 1000 should be used for silylation and chromatography of nucleosides in an RNA hydrolysate. As reported earlier the best derivatization of nucleosides was achieved using closed tube silylation at 150 degrees for 15 min with 225 molar excess BSTFA and chromatography on 4% OV-11 on Supelcoport. In general, the presence of salts and other substances can be significant in quantitative work, thus it is suggested that they be removed using chromatographic cleanup methods. The stability of nucleosides as a function of concentration of HCl, at room temperature was studied and very low RWR values for nucleosides were obtained when stored for 48 h in greater than 0.001 N HCl. Trimethylsilylation of various nucleotides and dinucleotides were made at 15 min as a function of temperature, and at 150 degrees at different times... | Derivatization and chromatography of nucleosides and nucleotides. The aims of this study were to determine the effect of levels of various substances and reaction by-products, which are formed during hydrolysis of nucleic acids, on the derivatization and chromatography of nucleosides; and to investigate the silylation of mono- and dinucleotides. The effect of NaCl, KCl, MgCl2, NH4Cl, and (NH4)2SO4 on silylation and chromatography of nucleosides was studies at various molar excesses of salt. The response values for all nucleosides were studied at various molar excesses of salt. The response values for all nucleosides were significantly affected at molar excess salt present values (MSP) between 1 and 10 for KCl, NaCl, NH4Cl, (NH4)2SO4 and between 0.1 and 1 for MgCl2. It was noted that thymidine was more sensitive than other nucleosides if silylated in presence of these salts. Two chromatographic peaks at retention temperatures (RT) 240 and 251 were obtained for cytidine at MSP values of 10(-3) for NaCl, KCl, and MgCl2, and 10(-4) for NH4Cl and (NH4)2SO4. In a mixture of nucleosides the RT = 251 peak was used for quantitative analysis of cytidine as the RT = 240 peak elutes with guanosine. Thus, these salts have a significant effect on the gas-liquid chromatography of trimethylsilyl (TMS) cytidine in a mixture of nucleosides, especially the RT = 241 peak. The effect of salts on derivatization can be explained in part as follows: (a) reduced derivatization of nucleosides due to a decreased solubility in the solvent system; (b) formation of TMS anion derivatives, e.g. TMS-SO4, TMS-PO4, with a reduced molar excess of BSTFA; (c) metal chelation by Mg ions or other divalent cations with nucleosides or BSTFA; and/or (d) an increased breakdown of TMS derivatives in presence of salt in the sample or on the top 3 in. of the column packing. Also, experiments were made on the effect of other substances such as Tris, phosphate, alkaline phosphatase, and KCl on completeness of silylation. The individual impurities showed no significant effect on the relative weight response (RWR) values of nucleosides; however, when a mixture was used, significantly lower RWR values were observed for all nucleosides except thymidine when using 1000 molar excess of BSTFA greater than 1000 should be used for silylation and chromatography of nucleosides in an RNA hydrolysate. As reported earlier the best derivatization of nucleosides was achieved using closed tube silylation at 150 degrees for 15 min with 225 molar excess BSTFA and chromatography on 4% OV-11 on Supelcoport. In general, the presence of salts and other substances can be significant in quantitative work, thus it is suggested that they be removed using chromatographic cleanup methods. The stability of nucleosides as a function of concentration of HCl, at room temperature was studied and very low RWR values for nucleosides were obtained when stored for 48 h in greater than 0.001 N HCl. Trimethylsilylation of various nucleotides and dinucleotides were made at 15 min as a function of temperature, and at 150 degrees at different times... | [
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|
PMID:16024 | Chromatographic separation of pyridine and adenine nucleotides on thin layers of poly(ethyleneimine) cellulose. | The chromatographic properties on thin layers of poly(ethyleneimine) cellulose of sixteen compounds containing the pyridine and/or adenine ring have been studied. Chromatographic mobilities have been examined as a function of the concentration of lithium chloride or sodium formate buffer in the chromatographic solvent. These data provide a rationale for the development of rapid and simple separation methods that should prove useful in the study of pyridine and adenine nucleotide metabolism. | Chromatographic separation of pyridine and adenine nucleotides on thin layers of poly(ethyleneimine) cellulose. The chromatographic properties on thin layers of poly(ethyleneimine) cellulose of sixteen compounds containing the pyridine and/or adenine ring have been studied. Chromatographic mobilities have been examined as a function of the concentration of lithium chloride or sodium formate buffer in the chromatographic solvent. These data provide a rationale for the development of rapid and simple separation methods that should prove useful in the study of pyridine and adenine nucleotide metabolism. | [
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|
PMID:16025 | Thin-layer chromatographic procedure for the detection, isolation and identification of basic psychotropic drugs in urine. | A procedure is described for the detection and identification of basic psychoactive drugs in urine. In the analytical system proposed, detection is dependent on thin-layer chromatography and chromophoric spraying of the resulting chromatogram. Identification is based on the extractability of the compound at the pH applied, on RF values in two solvents, on colour characteristics after exposure to a sequence of reagents, on fluorescence and UV-absorption characteristics, on retention times in different gas-liquid chromatographic systems and on the behaviour in ion-pair extraction with methyl orange. The procedure has been applied to some narcotic alkaloids and amines which exhibit central stimulant action. | Thin-layer chromatographic procedure for the detection, isolation and identification of basic psychotropic drugs in urine. A procedure is described for the detection and identification of basic psychoactive drugs in urine. In the analytical system proposed, detection is dependent on thin-layer chromatography and chromophoric spraying of the resulting chromatogram. Identification is based on the extractability of the compound at the pH applied, on RF values in two solvents, on colour characteristics after exposure to a sequence of reagents, on fluorescence and UV-absorption characteristics, on retention times in different gas-liquid chromatographic systems and on the behaviour in ion-pair extraction with methyl orange. The procedure has been applied to some narcotic alkaloids and amines which exhibit central stimulant action. | [
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|
PMID:16026 | [Thin-layer chromatography of active compounds from ointments and suppositories followed by direct quantitative analysis by remission (author's transl)]. | The paper describes a method for simultaneous thin-layer chromatographic separation of hydrocortisone, hydrocortisone acetate or hydrocortisone caproate alongside dibucaine hydrochloride, hexachlorophene and clemizole undecylate as well as clemizole hexachlorophenate in ointments and suppositories. Development of thin-layer chromatograms is carried out on silica gel 60 F-254 pre-coated plates. All four active ingredients can be separated on one silica gel plate using one solvent system and determined directly by the remission method using a densitometer. Hydrocortisone and its two esters are measured at 248 nm, dibucaine hydrochloride at 325 nm, hexachlorophene at 300 nm, and clemizole undecylate as well as clemizole hexachlorophenate at 275 nm. Evaluation of thin-layer chromatograms takes place on-line from a linear calibration curve using an IBM 1800 computer. The described method is very suitable for analyses of these active ingredients in drug forms, such as ointments or suppositories and is reproducible with coefficients of variation of 1.29-3.56%. | [Thin-layer chromatography of active compounds from ointments and suppositories followed by direct quantitative analysis by remission (author's transl)]. The paper describes a method for simultaneous thin-layer chromatographic separation of hydrocortisone, hydrocortisone acetate or hydrocortisone caproate alongside dibucaine hydrochloride, hexachlorophene and clemizole undecylate as well as clemizole hexachlorophenate in ointments and suppositories. Development of thin-layer chromatograms is carried out on silica gel 60 F-254 pre-coated plates. All four active ingredients can be separated on one silica gel plate using one solvent system and determined directly by the remission method using a densitometer. Hydrocortisone and its two esters are measured at 248 nm, dibucaine hydrochloride at 325 nm, hexachlorophene at 300 nm, and clemizole undecylate as well as clemizole hexachlorophenate at 275 nm. Evaluation of thin-layer chromatograms takes place on-line from a linear calibration curve using an IBM 1800 computer. The described method is very suitable for analyses of these active ingredients in drug forms, such as ointments or suppositories and is reproducible with coefficients of variation of 1.29-3.56%. | [
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|
PMID:16028 | Itaconic acid carrier ampholytes for isoelectric focusing. | Commercial carrier ampholytes, obtained by coupling polyethylene polyamines to acrylic acid, exhibit a conductivity minimum in the pH range 5.5-6.5 owing to the lack of appropriate pK values of the polyamine in this pH region. By replacing acrylic with itaconic acid, it has been possible to effect substantial improvements in the pH range 5.5-6.5 as itaconic acid has a pK2 value of 5.45. Upon coupling, the pK of the gramma-carboxyl group remains virtually unaltered. With itoconic acid carrier ampholytes it has been possible to improve the conductivity in the pH range 5.5-6.5 by as much as 400% compared with conventional carrier ampholytes. It is suggected that the commercial products should be supplemented with itaconic acid carrier ampholytes in order to obtain a more uniform conductivity and buffering capacity in the pH range 3-10. | Itaconic acid carrier ampholytes for isoelectric focusing. Commercial carrier ampholytes, obtained by coupling polyethylene polyamines to acrylic acid, exhibit a conductivity minimum in the pH range 5.5-6.5 owing to the lack of appropriate pK values of the polyamine in this pH region. By replacing acrylic with itaconic acid, it has been possible to effect substantial improvements in the pH range 5.5-6.5 as itaconic acid has a pK2 value of 5.45. Upon coupling, the pK of the gramma-carboxyl group remains virtually unaltered. With itoconic acid carrier ampholytes it has been possible to improve the conductivity in the pH range 5.5-6.5 by as much as 400% compared with conventional carrier ampholytes. It is suggected that the commercial products should be supplemented with itaconic acid carrier ampholytes in order to obtain a more uniform conductivity and buffering capacity in the pH range 3-10. | [
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|
PMID:16029 | Determination of clorazepate and its major metabolites in blood and urine by electron capture gas-liquid chromatography. | A sensitive and specific blood level method employing differential extraction was developed for the determination of clorazepate and its N-desmethyldiazepam metabolite by electron capture gas-liquid chromatography (GLC-ECD). The assay requires the initial extraction of N-desmethyldiazepam, the major metabolite, into benzene-methylene chloride (90:10) from the biological sample made alkaline with 0.1 N NaOH. The samples is then acidified with 2 N HCl to decarboxylate clorazepate to N-desmethyldiazepam, which is then extracted into benzene-methylene chloride (90:10) after adjusting the pH to 12.8 with NaOH. The two extracts are evaporated and the residues are dissolved in benzene which contains griseofulvin as the reference standard. These solutions are assayed by GLC-ECD. The overall recovery and sensitivity limit of the assay for clorazepate is 60+/-5% (S.D.) and 4.0 ng/ml blood, respectively, while that for N-desmethyldiazepam is 95+/-5% (S.D.) and 4.0 ng/ml blood, respectively. The urinary excretion of clorazepate was determined by the measurement of the levels of N-desmethyldiazepam and oxazepam, the major urinary metabolites of clorazepate, both prior to and after enzymatic deconjugation. These methods were applied to the measurement of clorazepate and its metabolites in blood and urine following a single 15-mg dose of clorazepate dipotassium. | Determination of clorazepate and its major metabolites in blood and urine by electron capture gas-liquid chromatography. A sensitive and specific blood level method employing differential extraction was developed for the determination of clorazepate and its N-desmethyldiazepam metabolite by electron capture gas-liquid chromatography (GLC-ECD). The assay requires the initial extraction of N-desmethyldiazepam, the major metabolite, into benzene-methylene chloride (90:10) from the biological sample made alkaline with 0.1 N NaOH. The samples is then acidified with 2 N HCl to decarboxylate clorazepate to N-desmethyldiazepam, which is then extracted into benzene-methylene chloride (90:10) after adjusting the pH to 12.8 with NaOH. The two extracts are evaporated and the residues are dissolved in benzene which contains griseofulvin as the reference standard. These solutions are assayed by GLC-ECD. The overall recovery and sensitivity limit of the assay for clorazepate is 60+/-5% (S.D.) and 4.0 ng/ml blood, respectively, while that for N-desmethyldiazepam is 95+/-5% (S.D.) and 4.0 ng/ml blood, respectively. The urinary excretion of clorazepate was determined by the measurement of the levels of N-desmethyldiazepam and oxazepam, the major urinary metabolites of clorazepate, both prior to and after enzymatic deconjugation. These methods were applied to the measurement of clorazepate and its metabolites in blood and urine following a single 15-mg dose of clorazepate dipotassium. | [
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|
PMID:16030 | Rapid and sensitive electron-capture gas chromatographic method for the determination of pinazepam and its metabolites in human plasma, urine and milk. | A rapid, sensitive and specific gas-liquid chromatographic method for the measurement of pinazepam and its metabolites in biological fluids is reported. After a single extraction of the sample with toluene, the organic phase is concentrated and, after chromatography on a 3% OV-17 column, measured with an electron-capture detector. The sensitivity was 1.0 ng/ml for pinazepam and 5.0 ng/ml for its metabolites. Plasma levels and urinary excretion in human volunteers and plasma and milk levels in women suffering from anxiety during breastfeeding are reported. | Rapid and sensitive electron-capture gas chromatographic method for the determination of pinazepam and its metabolites in human plasma, urine and milk. A rapid, sensitive and specific gas-liquid chromatographic method for the measurement of pinazepam and its metabolites in biological fluids is reported. After a single extraction of the sample with toluene, the organic phase is concentrated and, after chromatography on a 3% OV-17 column, measured with an electron-capture detector. The sensitivity was 1.0 ng/ml for pinazepam and 5.0 ng/ml for its metabolites. Plasma levels and urinary excretion in human volunteers and plasma and milk levels in women suffering from anxiety during breastfeeding are reported. | [
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|
PMID:16031 | Analysis of warfarin in plasma by high-pressure liquid chromatography. | An improved high-pressure liquid chromatography method for the estimation of warfarin in plasma was developed. Plasma was acidified and extracted with ethylene dichloride spiked with methylated warfarin [3-(alpha-acetonylbenzyl)-4-methoxy-coumarin] as internal standard. The residue, redissolved in dioxane, was chromatographed on a reversed-phase column using a mobile phase of 40% dioxane in water (pH 4.2) on a high-pressure liquid chromatograph fitted with an UV absorbance detector. Recoveries from extraction, quantitated using tracer amounts of [14C]warfarin and methylated [14C]warfarin were 92.2 +/- 3.16% and 82.33 +/- 1.03%, respectively. The standard curve was linear between o.625 and 5.0 microng/ml. Detection was sensitive to approximately 0.5 microng/ml and specific without the inter ference of normal plasma constituents and warfarin metabolites. | Analysis of warfarin in plasma by high-pressure liquid chromatography. An improved high-pressure liquid chromatography method for the estimation of warfarin in plasma was developed. Plasma was acidified and extracted with ethylene dichloride spiked with methylated warfarin [3-(alpha-acetonylbenzyl)-4-methoxy-coumarin] as internal standard. The residue, redissolved in dioxane, was chromatographed on a reversed-phase column using a mobile phase of 40% dioxane in water (pH 4.2) on a high-pressure liquid chromatograph fitted with an UV absorbance detector. Recoveries from extraction, quantitated using tracer amounts of [14C]warfarin and methylated [14C]warfarin were 92.2 +/- 3.16% and 82.33 +/- 1.03%, respectively. The standard curve was linear between o.625 and 5.0 microng/ml. Detection was sensitive to approximately 0.5 microng/ml and specific without the inter ference of normal plasma constituents and warfarin metabolites. | [
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|
PMID:16032 | Epidemiological studies of Streptococcus pneumoniae in infants: methods of isolating pneumococci. | A prospective study of the natural history of pneumococcal infection, which involves serial culture studies in healthy infants from 6 weeks of age onward, is in progress in our laboratory. This report describes results of a comparison of several methods for the isolation and identification of Streptococcus pneumoniae from the nasopharynges and throats of these infants. Sheep blood agar, sheep blood agar with gentamicin sulfate (gentamicin agar), and mouse inoculation with 4-h broth cultures were used. Gentamicin agar proved superior to plain sheep blood agar as a solid culture medium, especially in enhancing the recovery of pneumococci from throat cultures. With gentamicin agar, similar carrier rates were found for both culture sites (nasopharynx and throat). In addition, gentamicin agar proved superior to mouse inoculation for the recovery of carrier strains from 131 nasopharyngeal culture samples processed by both methods. Sixty of 131 samples were positive for pneumococci, 25% of which would have been missed had mouse inoculation alone been used. In only three instances did we recover a strain by mouse inoculation that failed to grow on gentamicin agar; conversely, 15 strains were isolated on gentamicin agar but could not be recovered from mice. The latter observation might be explained by the fact that certain carrier strains may be relatively mouse avirulent. The use of blood agar containing gentamicin appears to offer a simple and inexpensive method for the recovery of S. pneumoniae and, in our opinion, provides an ideal method for the identification of pneumococcal carriers as well as for the recovery of these strains from clinical material such as sputum or ear exudates, where other and less fastidious organisms may also be present. | Epidemiological studies of Streptococcus pneumoniae in infants: methods of isolating pneumococci. A prospective study of the natural history of pneumococcal infection, which involves serial culture studies in healthy infants from 6 weeks of age onward, is in progress in our laboratory. This report describes results of a comparison of several methods for the isolation and identification of Streptococcus pneumoniae from the nasopharynges and throats of these infants. Sheep blood agar, sheep blood agar with gentamicin sulfate (gentamicin agar), and mouse inoculation with 4-h broth cultures were used. Gentamicin agar proved superior to plain sheep blood agar as a solid culture medium, especially in enhancing the recovery of pneumococci from throat cultures. With gentamicin agar, similar carrier rates were found for both culture sites (nasopharynx and throat). In addition, gentamicin agar proved superior to mouse inoculation for the recovery of carrier strains from 131 nasopharyngeal culture samples processed by both methods. Sixty of 131 samples were positive for pneumococci, 25% of which would have been missed had mouse inoculation alone been used. In only three instances did we recover a strain by mouse inoculation that failed to grow on gentamicin agar; conversely, 15 strains were isolated on gentamicin agar but could not be recovered from mice. The latter observation might be explained by the fact that certain carrier strains may be relatively mouse avirulent. The use of blood agar containing gentamicin appears to offer a simple and inexpensive method for the recovery of S. pneumoniae and, in our opinion, provides an ideal method for the identification of pneumococcal carriers as well as for the recovery of these strains from clinical material such as sputum or ear exudates, where other and less fastidious organisms may also be present. | [
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|
PMID:16033 | PH metric method for the determination of nicotinic acid in plasma. | The acidimetric method for the determination of nicotinic acid (NA) using Lactobacillus plantarum ATCC 8014 (Lactobacillus arabinosus 17-5) has been simplified and thus made less time consuming, and the sensitivity has been increased fivefold by replacement of the titration by a pH determination. As the regression of the decrease in pH on the amount of NA was found linear within a range of 1 to 4 ng of NA per ml, the calculations were performed according to the slope-ratio principle. The NA concentration of plasma was determined with a coefficient of variation of 5 to 7%, which rose to about 10% at low NA concentrations. Assays of fasting plasma samples from 13 hyperlipidemic male patients showed a group mean NA concentration of 80 +/- 55 ng/ml (mean +/- 2 standard deviation), before treatment, and 705 +/- 544 ng/ml (mean +/- 2 standard deviation) during therapy with sustained release NA preparations, of which a single dose, ingested during steady-state conditions, doubled or tripled the plasma concentration within 1 to 3 h. | PH metric method for the determination of nicotinic acid in plasma. The acidimetric method for the determination of nicotinic acid (NA) using Lactobacillus plantarum ATCC 8014 (Lactobacillus arabinosus 17-5) has been simplified and thus made less time consuming, and the sensitivity has been increased fivefold by replacement of the titration by a pH determination. As the regression of the decrease in pH on the amount of NA was found linear within a range of 1 to 4 ng of NA per ml, the calculations were performed according to the slope-ratio principle. The NA concentration of plasma was determined with a coefficient of variation of 5 to 7%, which rose to about 10% at low NA concentrations. Assays of fasting plasma samples from 13 hyperlipidemic male patients showed a group mean NA concentration of 80 +/- 55 ng/ml (mean +/- 2 standard deviation), before treatment, and 705 +/- 544 ng/ml (mean +/- 2 standard deviation) during therapy with sustained release NA preparations, of which a single dose, ingested during steady-state conditions, doubled or tripled the plasma concentration within 1 to 3 h. | [
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|
PMID:16034 | Detection of pneumococci in respiratory secretions: clinical evaluation of gentamicin blood agar. | The use of sheep blood agar containing 5 microng of gentamicin per ml has been suggested as a means of selectively isolating Streptococcus pneumoniae from respiratory secretions. We have tested this method, in parallel with standard methods, on 844 respiratory specimens in a clinical laboratory and have confirmed that the yield of pneumococci can be increased approximately 40% by using agar containing gentamicin. However, since the antibiotic suppresses the growth of staphylococci, group A streptococci, and gram-negative bacilli, gentamicin agar cannot be used as a replacement for the standard method. The requirement for duplicate plating raises the cost per additional pneumococcal isolate to prohibitive amounts. Although the method is useful in studies designed to isolate only pneumococci, it cannot be recommended for the routine clinical laboratory. An unanticipated observation from our study is that the yield of pneumococci in respiratory secretions can be increased 10-fold simply by screening sputum for the presence of leukocytes using the Gram stain. This is in agreement with results reported from other laboratories. | Detection of pneumococci in respiratory secretions: clinical evaluation of gentamicin blood agar. The use of sheep blood agar containing 5 microng of gentamicin per ml has been suggested as a means of selectively isolating Streptococcus pneumoniae from respiratory secretions. We have tested this method, in parallel with standard methods, on 844 respiratory specimens in a clinical laboratory and have confirmed that the yield of pneumococci can be increased approximately 40% by using agar containing gentamicin. However, since the antibiotic suppresses the growth of staphylococci, group A streptococci, and gram-negative bacilli, gentamicin agar cannot be used as a replacement for the standard method. The requirement for duplicate plating raises the cost per additional pneumococcal isolate to prohibitive amounts. Although the method is useful in studies designed to isolate only pneumococci, it cannot be recommended for the routine clinical laboratory. An unanticipated observation from our study is that the yield of pneumococci in respiratory secretions can be increased 10-fold simply by screening sputum for the presence of leukocytes using the Gram stain. This is in agreement with results reported from other laboratories. | [
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|
PMID:16035 | Reactivation of Newcastle Disease Virus Neutralized by Antibody. | In an effort to improve current technology for detection of Newcastle disease virus in convalescent birds, a procedure has been developed for efficient reactivation of virus that has been neutralized by antibody. The reactivation capabilities of fluorocarbon treatment, ultrasonic treatment, pH extremes, and proteolytic digestion were evaluated using the LaSota strain of virus. Reactivation was maximum after proteolytic digestion with either trypsin or papain, and reactivation effciency was up to 100%, depending on the enzyme used for digestion and the amount of antibody in the neutralization mixture. Reactivation at pH extremes was considerably less efficient than reactiviation by proteolytic digestion, and neither fluorocarbon nor ultrasonic treatments effectively recovered antibody-neutralized Newcastle disease virus. | Reactivation of Newcastle Disease Virus Neutralized by Antibody. In an effort to improve current technology for detection of Newcastle disease virus in convalescent birds, a procedure has been developed for efficient reactivation of virus that has been neutralized by antibody. The reactivation capabilities of fluorocarbon treatment, ultrasonic treatment, pH extremes, and proteolytic digestion were evaluated using the LaSota strain of virus. Reactivation was maximum after proteolytic digestion with either trypsin or papain, and reactivation effciency was up to 100%, depending on the enzyme used for digestion and the amount of antibody in the neutralization mixture. Reactivation at pH extremes was considerably less efficient than reactiviation by proteolytic digestion, and neither fluorocarbon nor ultrasonic treatments effectively recovered antibody-neutralized Newcastle disease virus. | [
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|
PMID:16036 | Rapid method for determining nitrate utilization by yeasts. | A test for the nitrate-reductase activity in yeasts has been developed, in which the reaction may be read after only 10 min of incubation. The rapidity of the test is due to the optimization of pH, substrate concentration, and temperature for the reaction. | Rapid method for determining nitrate utilization by yeasts. A test for the nitrate-reductase activity in yeasts has been developed, in which the reaction may be read after only 10 min of incubation. The rapidity of the test is due to the optimization of pH, substrate concentration, and temperature for the reaction. | [
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|
PMID:16037 | Intrarenal dynamics in the pathogenesis and prevention of acute urate nephropathy. | Tubular fluid flow, urine osmolality, and pH were selectively altered to determine the relative protective roles of these factors in a rat model of acute urate nephrophathy. Various prehyper uricemic conditions were established in five groups of animals: (a) normopenic Wistar rats given no pretreatment (Group I); (b) Wistar rats given acetazolamide, 20 mg/kg, and isotonic NaHCO3 to produce urine alkalinization (Group II); (c) Wistar rats in which a moderate diuresis, similar to that observed in Group II but without urine alkalinization, was induced with furosemide, 2 mg/kg (Group III); (d) Wistar rats in which a high-flow solute diuresis was induced with furosemide, 15 mg/kg (Group IV); (e) Brattleboro rats, homozygous for pituitary diabetes insipidus, that had a spontaneous high-flow water diuresis (Group V). A comparable level of hyperuricemia (19.4+/-2.2 mg/100 ml) was achieved in all animals with intravenous urate infusion. Clearance and micropuncture studies were performed before and 1 h after induction of hyperuicemia. Group I rats had mean falls in renal plasma flow and glomerular filtration rate of 83 and 86%, respectively; nephron filtration rate decreased 66%, and tubular and microvascular pressures increased twofold. In Group II there were 45 and 47% declines in renal plasma flow and glomerular filtration rate, respectively, a 66% fall in nephron filtration rate, and a 30% increase in tubular and vascular pressures. Moderate amounts of urate were seen in the kidneys. Group III had changes in renal function identical to Group II suggesting that the moderate prehyperuricemic diuresis in the latter group and not urine alkalinization produced the partial protection observed. Groups IV and V were completely and comparably protected with renal function studies unchanged from controls. It is concluded that high tubular fluid flow, whether induced by a solute or water diuresis, is the primary mechanism of protection in acute urate nephropathy. At most, urine alkalinization plays a minor preventive role. | Intrarenal dynamics in the pathogenesis and prevention of acute urate nephropathy. Tubular fluid flow, urine osmolality, and pH were selectively altered to determine the relative protective roles of these factors in a rat model of acute urate nephrophathy. Various prehyper uricemic conditions were established in five groups of animals: (a) normopenic Wistar rats given no pretreatment (Group I); (b) Wistar rats given acetazolamide, 20 mg/kg, and isotonic NaHCO3 to produce urine alkalinization (Group II); (c) Wistar rats in which a moderate diuresis, similar to that observed in Group II but without urine alkalinization, was induced with furosemide, 2 mg/kg (Group III); (d) Wistar rats in which a high-flow solute diuresis was induced with furosemide, 15 mg/kg (Group IV); (e) Brattleboro rats, homozygous for pituitary diabetes insipidus, that had a spontaneous high-flow water diuresis (Group V). A comparable level of hyperuricemia (19.4+/-2.2 mg/100 ml) was achieved in all animals with intravenous urate infusion. Clearance and micropuncture studies were performed before and 1 h after induction of hyperuicemia. Group I rats had mean falls in renal plasma flow and glomerular filtration rate of 83 and 86%, respectively; nephron filtration rate decreased 66%, and tubular and microvascular pressures increased twofold. In Group II there were 45 and 47% declines in renal plasma flow and glomerular filtration rate, respectively, a 66% fall in nephron filtration rate, and a 30% increase in tubular and vascular pressures. Moderate amounts of urate were seen in the kidneys. Group III had changes in renal function identical to Group II suggesting that the moderate prehyperuricemic diuresis in the latter group and not urine alkalinization produced the partial protection observed. Groups IV and V were completely and comparably protected with renal function studies unchanged from controls. It is concluded that high tubular fluid flow, whether induced by a solute or water diuresis, is the primary mechanism of protection in acute urate nephropathy. At most, urine alkalinization plays a minor preventive role. | [
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|
PMID:16038 | Hydrolysis of the elastase substrate succinyltrialanine nitroanilide by a metal-dependent enzyme in rheumatoid synovial fluid. | A new type of enzyme hydrolyzing the elastase substrate succinyl-L-alanyl-L-alanine-4-nitroanilide has been found in cell-free rheuma todi synovial fluid. Normal plasma and osteoarthritic synovial fluid contained relatively little enzyme. The pH optimum was 8.0. Unexpectedly, the enzyme activity was not due to leukocyte elastase or any proteinase bound to alpha2-macroglobulin. The enzyme activity was metal-dependent being inhibited by chelating agents but not by di-isopropylfluorophos phate or thiol-blocking reagents. Gel chromatography showed the enzyme activity was associated with material of high molecular weight. On Sepharose 4B chromatography two-thirds of the activity eluted in the void volume and one-third in a position of about 106 mol wt. Utracentrifugation showed that both components were associated with lipid. The buoyant density of the higher molecular weight material was 1.15-1.22 g/ml., and that of lower molecular weight material was 1.2-1.33 g/ml. No latency of the enzyme was revealed by freezing and thawing or treatment with detergents. The nature of the enzyme is discussed. It is likely to be a proteinase possibly bound to some kind of membrane fragment. | Hydrolysis of the elastase substrate succinyltrialanine nitroanilide by a metal-dependent enzyme in rheumatoid synovial fluid. A new type of enzyme hydrolyzing the elastase substrate succinyl-L-alanyl-L-alanine-4-nitroanilide has been found in cell-free rheuma todi synovial fluid. Normal plasma and osteoarthritic synovial fluid contained relatively little enzyme. The pH optimum was 8.0. Unexpectedly, the enzyme activity was not due to leukocyte elastase or any proteinase bound to alpha2-macroglobulin. The enzyme activity was metal-dependent being inhibited by chelating agents but not by di-isopropylfluorophos phate or thiol-blocking reagents. Gel chromatography showed the enzyme activity was associated with material of high molecular weight. On Sepharose 4B chromatography two-thirds of the activity eluted in the void volume and one-third in a position of about 106 mol wt. Utracentrifugation showed that both components were associated with lipid. The buoyant density of the higher molecular weight material was 1.15-1.22 g/ml., and that of lower molecular weight material was 1.2-1.33 g/ml. No latency of the enzyme was revealed by freezing and thawing or treatment with detergents. The nature of the enzyme is discussed. It is likely to be a proteinase possibly bound to some kind of membrane fragment. | [
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|
PMID:16040 | Metabolic studies in patients with nadolol: oral and intravenous administration. | Nadolol-14C, 2,3-cis-5-(3-[(1,1-dimethylethyl)amino]-2-hydroxypropoxy)-1,2,3,4-tetrahydro-2,3-naphthalenediol, a nonselective beta-adrenergic blocking agent, was administered orally and intravenously at 2-mg doses to patients with mild cases of essential hypertension. Terminal plasma half-times after oral and intravenous doses were an average of 12.2 and 9.8 hours, respectively. After oral doses, an average of 24.6 and 76.9 per cent of the dose was excreted in urine and feces, respectively, whereas, after intravenous doses, an average of 72.9 and 23.3 per cent of the dose was excreted by the same routes. Calculations of absorption, based on urinary excretion and on areas under the plasma concentration-versus-time curves, indicated that oral doses of nadolol-14C were absorbed to the extent of 33.6+/-2.4 per cent (+/- S.E.). The average overall volume of distribution after intravenous administration was 2.09+/-0.51 1./kg (+/- S.E.), and the average volume of the central compartment was 0.30+/-0.04 1./kg. Only unchanged nadolol-14C was excreted in the urine and feces of patients after either oral or intravenous administration of the drug. | Metabolic studies in patients with nadolol: oral and intravenous administration. Nadolol-14C, 2,3-cis-5-(3-[(1,1-dimethylethyl)amino]-2-hydroxypropoxy)-1,2,3,4-tetrahydro-2,3-naphthalenediol, a nonselective beta-adrenergic blocking agent, was administered orally and intravenously at 2-mg doses to patients with mild cases of essential hypertension. Terminal plasma half-times after oral and intravenous doses were an average of 12.2 and 9.8 hours, respectively. After oral doses, an average of 24.6 and 76.9 per cent of the dose was excreted in urine and feces, respectively, whereas, after intravenous doses, an average of 72.9 and 23.3 per cent of the dose was excreted by the same routes. Calculations of absorption, based on urinary excretion and on areas under the plasma concentration-versus-time curves, indicated that oral doses of nadolol-14C were absorbed to the extent of 33.6+/-2.4 per cent (+/- S.E.). The average overall volume of distribution after intravenous administration was 2.09+/-0.51 1./kg (+/- S.E.), and the average volume of the central compartment was 0.30+/-0.04 1./kg. Only unchanged nadolol-14C was excreted in the urine and feces of patients after either oral or intravenous administration of the drug. | [
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|
PMID:16044 | Electroencephalographic responses to photic stimulation in habitual smokers and nonsmokers. | Two studies are reported in which electroencephalograms (EEGs) of habitual cigarette smokers and of nonsmokers were taken before and after they were required to smoke a cigarette. The EEGs were scored for incidence of EEG "driving" responses to photic stimulation, an index that appears to reflect the balance between central adrenergic and cholinergic nervous systems. The findings suggest that smokers tend to have a central autonomic balance less in favor of adrenergic functioning than do nonsmokers. Cigarette smoking may alleviate a possible central adrenergic insufficiency of smokers. These findings suggest a solution to "Nesbitt's paradox," which has reference to the fact that while nicotine is a central adrenergic stimulant, smokers describe the effect of smoking in sedational terms (i.e., as relaxing or calming). | Electroencephalographic responses to photic stimulation in habitual smokers and nonsmokers. Two studies are reported in which electroencephalograms (EEGs) of habitual cigarette smokers and of nonsmokers were taken before and after they were required to smoke a cigarette. The EEGs were scored for incidence of EEG "driving" responses to photic stimulation, an index that appears to reflect the balance between central adrenergic and cholinergic nervous systems. The findings suggest that smokers tend to have a central autonomic balance less in favor of adrenergic functioning than do nonsmokers. Cigarette smoking may alleviate a possible central adrenergic insufficiency of smokers. These findings suggest a solution to "Nesbitt's paradox," which has reference to the fact that while nicotine is a central adrenergic stimulant, smokers describe the effect of smoking in sedational terms (i.e., as relaxing or calming). | [
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|
PMID:16039 | A method for evaluating anxiolytic sedatives. | Although anxiolytic sedatives are widely used in clinical practice, the methodology for assessing treatment effect of these compounds has not been well developed. The present double-blind study was designed to refine methodology for evaluating anxiolytics. Choice of rating scale, patient selection, maintenance of the double-blind status, the subjects' environment during the study, and the subjects' understanding of the study are discussed as considerations in reducing sources of variability and bias in the study of anxiolytics. After placebo prescreening, 14 subjects with diagnoses of anxiety recieved 3 to 6 mg lorazepam daily for four weeks, while 14 control subjects received placebo. The Hamilton Anxiety Rating Scale (HARS) and the Wang Anxiety Rating Scale (WARS), with its Anxiolytic Adjunct Scale (AAS), were used to assess changes in anxiety. The Wang and Hamilton ratings correlated well at both comparison periods. Lorazepam demonstrated significant superiority to placebo and produced no serious adverse effects. Anxiolytic efficacy did not differ significantly among the four weekly ratings. | A method for evaluating anxiolytic sedatives. Although anxiolytic sedatives are widely used in clinical practice, the methodology for assessing treatment effect of these compounds has not been well developed. The present double-blind study was designed to refine methodology for evaluating anxiolytics. Choice of rating scale, patient selection, maintenance of the double-blind status, the subjects' environment during the study, and the subjects' understanding of the study are discussed as considerations in reducing sources of variability and bias in the study of anxiolytics. After placebo prescreening, 14 subjects with diagnoses of anxiety recieved 3 to 6 mg lorazepam daily for four weeks, while 14 control subjects received placebo. The Hamilton Anxiety Rating Scale (HARS) and the Wang Anxiety Rating Scale (WARS), with its Anxiolytic Adjunct Scale (AAS), were used to assess changes in anxiety. The Wang and Hamilton ratings correlated well at both comparison periods. Lorazepam demonstrated significant superiority to placebo and produced no serious adverse effects. Anxiolytic efficacy did not differ significantly among the four weekly ratings. | [
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|
PMID:16041 | Comparison of triazolam, flurazepam, and placebo as hypnotics in geriatric patients with insomnia. | The safety and efficacy of 0.25 mg triazolam were compared to those of 15 mg flurazepam and placebo in 41 geriatric outpatients suffering from insomnia. The patients were randomly assigned to one of the three treatment groups. The medication was taken at bedtime for 28 days. Tolerance development was also studied. Triazolam was found to be significantly better than placebo in how much the medication helped the patients sleep, in sleep onset, in duration of sleep, number of nighttime awakenings, in quality (depth) of sleep, and in feeling of restfulness in the morning. Triazolam was significantly better than flurazepam in duration of sleep and was rated higher than flurazepam in all other variables. Flurazepam was significantly better than placebo in only two variables--onset of sleep and quality (depth) of sleep. Side effects were reported in each treatment group, and one patient on placebo discontinued because of side effects. There was no decrease in hypnotic effect over this four-week period, therefore, no evidence of tolerance development on either of the active compounds. Both active compounds provided the same amount of relief from insomnia after four weeks as they had after one week. Laboratory analyses and poststudy physical examinations showed no deleterious effects over the four-week period. | Comparison of triazolam, flurazepam, and placebo as hypnotics in geriatric patients with insomnia. The safety and efficacy of 0.25 mg triazolam were compared to those of 15 mg flurazepam and placebo in 41 geriatric outpatients suffering from insomnia. The patients were randomly assigned to one of the three treatment groups. The medication was taken at bedtime for 28 days. Tolerance development was also studied. Triazolam was found to be significantly better than placebo in how much the medication helped the patients sleep, in sleep onset, in duration of sleep, number of nighttime awakenings, in quality (depth) of sleep, and in feeling of restfulness in the morning. Triazolam was significantly better than flurazepam in duration of sleep and was rated higher than flurazepam in all other variables. Flurazepam was significantly better than placebo in only two variables--onset of sleep and quality (depth) of sleep. Side effects were reported in each treatment group, and one patient on placebo discontinued because of side effects. There was no decrease in hypnotic effect over this four-week period, therefore, no evidence of tolerance development on either of the active compounds. Both active compounds provided the same amount of relief from insomnia after four weeks as they had after one week. Laboratory analyses and poststudy physical examinations showed no deleterious effects over the four-week period. | [
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|
PMID:16048 | The use of drugs for behavior modification as it relates to the practice of optometry--Part II. | Drugs used in behavior modification are considered with respect to type, specific agents, conditions for which they are used, and associated ocular and visual side effects. Relevant types include narcotic analgesics, sedatives and hypnotics, antipsychotics, antianxiety drugs, antidepressants, psychomotor stimulating agents, caffeine, the antihistamines, estrogen and progestins, vitamins, disulfiram, and illicit drugs and chemicals. | The use of drugs for behavior modification as it relates to the practice of optometry--Part II. Drugs used in behavior modification are considered with respect to type, specific agents, conditions for which they are used, and associated ocular and visual side effects. Relevant types include narcotic analgesics, sedatives and hypnotics, antipsychotics, antianxiety drugs, antidepressants, psychomotor stimulating agents, caffeine, the antihistamines, estrogen and progestins, vitamins, disulfiram, and illicit drugs and chemicals. | [
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|
PMID:16053 | Burns of the foot. | The most severe trauma a patient can sustain is a major burn. When a person is seriously burned, initial care begins with maintaining an adequate airway and adequate blood volume and urinary output by intravenous fluids. After the patient has been stabilized, the wound is of primary importance, and postage stamp split thickness grafts are used for skin coverage. When these are secure and a maximal range of motion has been obtained, reconstructive procedures should be started. | Burns of the foot. The most severe trauma a patient can sustain is a major burn. When a person is seriously burned, initial care begins with maintaining an adequate airway and adequate blood volume and urinary output by intravenous fluids. After the patient has been stabilized, the wound is of primary importance, and postage stamp split thickness grafts are used for skin coverage. When these are secure and a maximal range of motion has been obtained, reconstructive procedures should be started. | [
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|
PMID:16055 | Soft tissue trauma of the foot. | Before and since podiatric physicians began treating patients with foot ailments, soft tissue trauma has been a major challenge. Soft tissues, the outermost tissues, are traumatized with more ease and frequency than are skeletal tissues within. Management of soft tissue trauma must be deliberate and directed toward not only immediate, but also long-term results. Timing and expertise in management are essential for the successful treatment of soft tissue trauma of the foot. | Soft tissue trauma of the foot. Before and since podiatric physicians began treating patients with foot ailments, soft tissue trauma has been a major challenge. Soft tissues, the outermost tissues, are traumatized with more ease and frequency than are skeletal tissues within. Management of soft tissue trauma must be deliberate and directed toward not only immediate, but also long-term results. Timing and expertise in management are essential for the successful treatment of soft tissue trauma of the foot. | [
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|
PMID:16057 | [Pendulum testes: a degraded from of cryptorchism]. | In 22 cases of sterility we have been able to single out under the name of "pendulum testes" a syndrome showing the following features: --clinically, testes that are often small and soft and normally found in the lower part of the scrotum, but with a tendency to ride up toward the inguinal canal and stay there so that an attempt to bring them down manually into the scrotum in unsuccessful; --cytologically, often accompanied by very poor sperm formation, and; --histologically, showing tubule pathology. We approach this picture as that of crytorchidism for in our opinion pendulum testis is a degraded form of latter. This leads us to discuss for both conditions problems of classification and indications for treatment. | [Pendulum testes: a degraded from of cryptorchism]. In 22 cases of sterility we have been able to single out under the name of "pendulum testes" a syndrome showing the following features: --clinically, testes that are often small and soft and normally found in the lower part of the scrotum, but with a tendency to ride up toward the inguinal canal and stay there so that an attempt to bring them down manually into the scrotum in unsuccessful; --cytologically, often accompanied by very poor sperm formation, and; --histologically, showing tubule pathology. We approach this picture as that of crytorchidism for in our opinion pendulum testis is a degraded form of latter. This leads us to discuss for both conditions problems of classification and indications for treatment. | [
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|
PMID:16060 | An evaluation of elution techniques in the study of immune complex glomerulonephritis. | Antigen and antibody from glomerular immune complex deposits in rabbits with experimental bovine serum albumin-(BSA) induced chronic serum sickness (CSS) were quantitated in elutes from kidneys in which a portion of the antigen and antibody had been radiolabeled. The largest quantities of 125I BSA eluted with 1 M roprionic acid at pH 2.7 (86%) and 0.1 M borate buffer at pH 11.25 (80%). However, these buffers yielded less functional anti-BSA antibody than 0.02 M citrate buffer at pH 3.2 (344 mug/g kidney). Citrate buffer-eluted anti-BSA antibody was reactive in immunodiffusion, immunofluorescence, and radiolabeled BSA binding test systems, but complement fixation was impaired relative to chaotropic ion-eluted antibody. It was found that up to 75% of the eluted antibody was lost to further study by recombination with eluted BSA. This could be prevented by fractionation of the dissociated eluate before neutralization. IgG fractionated eluates were successfully fluorescein conjugated or radiolabeled for use as reagents. Elution of cryostat sections of CSS kidney was also studied; BSA, IgG, and complement (C3) eluted in parallel, and sub-microgram quantities of anti-BSA antibody were recovered. | An evaluation of elution techniques in the study of immune complex glomerulonephritis. Antigen and antibody from glomerular immune complex deposits in rabbits with experimental bovine serum albumin-(BSA) induced chronic serum sickness (CSS) were quantitated in elutes from kidneys in which a portion of the antigen and antibody had been radiolabeled. The largest quantities of 125I BSA eluted with 1 M roprionic acid at pH 2.7 (86%) and 0.1 M borate buffer at pH 11.25 (80%). However, these buffers yielded less functional anti-BSA antibody than 0.02 M citrate buffer at pH 3.2 (344 mug/g kidney). Citrate buffer-eluted anti-BSA antibody was reactive in immunodiffusion, immunofluorescence, and radiolabeled BSA binding test systems, but complement fixation was impaired relative to chaotropic ion-eluted antibody. It was found that up to 75% of the eluted antibody was lost to further study by recombination with eluted BSA. This could be prevented by fractionation of the dissociated eluate before neutralization. IgG fractionated eluates were successfully fluorescein conjugated or radiolabeled for use as reagents. Elution of cryostat sections of CSS kidney was also studied; BSA, IgG, and complement (C3) eluted in parallel, and sub-microgram quantities of anti-BSA antibody were recovered. | [
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|
PMID:16061 | Studies on cellular inhibition and serum-blocking factors in 28 human patients given marrow grafts from HLA identical siblings. | Fifteen patients with aplastic anemia and 13 with acute leukemia were studied 36 to 1547 days after treatment with high-dose cyclophosphamide and/or total-body irradiation and marrow transplantation from HLA identical siblings. Peripheral blood lymphocytes from patients and normals (marrow donors and healthy unrelated individuals) were tested for cell inhibition (CI) of cultured skin fibroblasts from both patients and donors by using the microcytotoxicity assay. In addition, blocking of CI by factors in patient serum was studied. Three groups of patients were studied. Patients in group I were stable long-term survivors without evidence of graft-vs-host diseases (GVHD) between 250 to 1547 days postgrafting. Patients in group II were short-term survivors with or without acute GVHD between 36 and 144 days postgrafting. Patients in group III had chronic GVHD either at the time of testing or developed chronic GVHD subsequent to CI testing between days 61 and 960 postgrafting. Eleven of 14 patients in group I showed absence of both CI and serum blocking and three showed CI and blocking. Patients in group II without acute GVHD showed absence of CI and serum blocking on three occasions, presence of CI and blocking on four occasions, and CI without blocking on three occasions. Patients in group II with acute GVHD showed absence of CI on one occasion and presence of CI and blocking on three occasions. Patients in group III showed absence of CI and blocking on seven occasions and CI without blocking on two occasions. These results suggest that the maintenance of stable graft-host tolerance in long-term survivors after marrow grafting from HLA identical donors does not depend on the presence of serum-blocking factors. Short-term survivors with and without GVHD showed a spectrum of in vitro reactivity with 50% of the patients showing serum-blocking factors, and these results did not appear to be correlated with presence or absence of acute GVHD. Finally, results of the microcytotoxicity assays failed to provide insight into the mechanism of chronic GVHD. | Studies on cellular inhibition and serum-blocking factors in 28 human patients given marrow grafts from HLA identical siblings. Fifteen patients with aplastic anemia and 13 with acute leukemia were studied 36 to 1547 days after treatment with high-dose cyclophosphamide and/or total-body irradiation and marrow transplantation from HLA identical siblings. Peripheral blood lymphocytes from patients and normals (marrow donors and healthy unrelated individuals) were tested for cell inhibition (CI) of cultured skin fibroblasts from both patients and donors by using the microcytotoxicity assay. In addition, blocking of CI by factors in patient serum was studied. Three groups of patients were studied. Patients in group I were stable long-term survivors without evidence of graft-vs-host diseases (GVHD) between 250 to 1547 days postgrafting. Patients in group II were short-term survivors with or without acute GVHD between 36 and 144 days postgrafting. Patients in group III had chronic GVHD either at the time of testing or developed chronic GVHD subsequent to CI testing between days 61 and 960 postgrafting. Eleven of 14 patients in group I showed absence of both CI and serum blocking and three showed CI and blocking. Patients in group II without acute GVHD showed absence of CI and serum blocking on three occasions, presence of CI and blocking on four occasions, and CI without blocking on three occasions. Patients in group II with acute GVHD showed absence of CI on one occasion and presence of CI and blocking on three occasions. Patients in group III showed absence of CI and blocking on seven occasions and CI without blocking on two occasions. These results suggest that the maintenance of stable graft-host tolerance in long-term survivors after marrow grafting from HLA identical donors does not depend on the presence of serum-blocking factors. Short-term survivors with and without GVHD showed a spectrum of in vitro reactivity with 50% of the patients showing serum-blocking factors, and these results did not appear to be correlated with presence or absence of acute GVHD. Finally, results of the microcytotoxicity assays failed to provide insight into the mechanism of chronic GVHD. | [
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|
PMID:16062 | Characteristics of tyrosinase in B16 melanoma. | Tyrosine hydroxylase, dopa oxidase, and peroxidase activities were studied in soluble fractions of B16 melanoma tumor homogenates by polyacrylamide gel disc electrophoresis. Stained gels were scanned photometrically and gel slices were assayed radiometrically. In these preparations, the two bands of tyrosine hydroxylating activity were completely separated from the peroxidase activity but coincided with two major bands of dopa oxidase activity. The third dopa oxidase band coincided with the single band of peroxidase activity. The soluble fraction of cultured cell homogenates had no peroxidase activity, but the two tyrosine hydroxylase bands coincided exactly with the two dopa oxidase bands. Therefore, in the soluble fraction of the murine melanoma bifunctional tyrosinase does exist as two electrophoretically separable forms which are independent of peroxidase. | Characteristics of tyrosinase in B16 melanoma. Tyrosine hydroxylase, dopa oxidase, and peroxidase activities were studied in soluble fractions of B16 melanoma tumor homogenates by polyacrylamide gel disc electrophoresis. Stained gels were scanned photometrically and gel slices were assayed radiometrically. In these preparations, the two bands of tyrosine hydroxylating activity were completely separated from the peroxidase activity but coincided with two major bands of dopa oxidase activity. The third dopa oxidase band coincided with the single band of peroxidase activity. The soluble fraction of cultured cell homogenates had no peroxidase activity, but the two tyrosine hydroxylase bands coincided exactly with the two dopa oxidase bands. Therefore, in the soluble fraction of the murine melanoma bifunctional tyrosinase does exist as two electrophoretically separable forms which are independent of peroxidase. | [
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|
PMID:16063 | Epidermal nucleases. II. The multiplicity of ribonucleases in guinea-pig epidermis. | Ribonuclease activity has been extracted from adult guinea-pig epidermis by sequential homogenization in dilute sodium acetate and sulfuric acid. The extracts were subjected to ammonium sulfate fractionation and to affinity and ion exchange chromatography. Three ribonucleases (I, II, III) were separated from the sodium acetate extract and 6(A, B1, B2, B3, C, D) were isolated from the sulfuric acid extract. The degree of purification varies from 65-fold to 8,700-fold and the apparent molecular weights of the active forms of 8 of the 9 ribonucleases range from 10,000 to 36,500. No phosphodiesterase activity is present in any of the 9 fractions, but there is alkaline phosphatase activity in one (I) and deoxyribonuclease activity in a second (B3). Two of the ribonucleases have acid pH optima (a1, B3), while the others are most active between PHs 6.8 and 7.8. The activity of 4 of the fractions is sensitive to added EDTA (III, A, B2, B3,), but no stimulatory metal ions were found. Low concentrations of the polyamine spermidine enhanced the activity of 3-fractions (III, C, D). Yeast ribonucleic acid is degraded exonucleolytically by 2 fractions (I, A) and endonucleolytically by the remaining 7. In experiments with homopolyribonucleotide substrates, poly U was generally the preferred substrate. Substantial hydrolysis of poly A occurred with 2 fractions (A, B3) and slight hydrolysis of poly G with 2 other fractions (B2, C). | Epidermal nucleases. II. The multiplicity of ribonucleases in guinea-pig epidermis. Ribonuclease activity has been extracted from adult guinea-pig epidermis by sequential homogenization in dilute sodium acetate and sulfuric acid. The extracts were subjected to ammonium sulfate fractionation and to affinity and ion exchange chromatography. Three ribonucleases (I, II, III) were separated from the sodium acetate extract and 6(A, B1, B2, B3, C, D) were isolated from the sulfuric acid extract. The degree of purification varies from 65-fold to 8,700-fold and the apparent molecular weights of the active forms of 8 of the 9 ribonucleases range from 10,000 to 36,500. No phosphodiesterase activity is present in any of the 9 fractions, but there is alkaline phosphatase activity in one (I) and deoxyribonuclease activity in a second (B3). Two of the ribonucleases have acid pH optima (a1, B3), while the others are most active between PHs 6.8 and 7.8. The activity of 4 of the fractions is sensitive to added EDTA (III, A, B2, B3,), but no stimulatory metal ions were found. Low concentrations of the polyamine spermidine enhanced the activity of 3-fractions (III, C, D). Yeast ribonucleic acid is degraded exonucleolytically by 2 fractions (I, A) and endonucleolytically by the remaining 7. In experiments with homopolyribonucleotide substrates, poly U was generally the preferred substrate. Substantial hydrolysis of poly A occurred with 2 fractions (A, B3) and slight hydrolysis of poly G with 2 other fractions (B2, C). | [
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PMID:16064 | Temperature-sensitive mutants of Streptococcus pneumoniae. I. Preparation and characterization in vitro of temperature-sensitive mutants of type I S. pneumoniae. | After exposure of type I Streptococcus pneumoniae to nitrosoguanidine, 13 temperature-sensitive (ts) mutants were selected that were restricted in capacity to form colonies on blood agar at 38 C. Whereas colony formation by the type I parent (ts+) was unaffected by a temperature of as high as 39 C, the ts mutants exhibited a spectrum of temperature sensitivity in which colony formation was inhibited significantly at 36 C, 37 C, 38 C, or 39 C. Growth of ts mutants at 38 C in broth was reduced or delayed relative to that of ts organisms under identical conditions. In general, there was a direct correlation between degree of temperature sensitivity and genetic stability. Mutants grown at a permissive temperature resembled the ts+ type I parent in colonial morphology and properties of alpha-hemolysis, bile solubility, optochin sensitivity, and antibiotic sensitivity. Moreover, in vitro studies indicated that the mutants retained capsules of immunochemically reactive type I capsular polysaccharide. | Temperature-sensitive mutants of Streptococcus pneumoniae. I. Preparation and characterization in vitro of temperature-sensitive mutants of type I S. pneumoniae. After exposure of type I Streptococcus pneumoniae to nitrosoguanidine, 13 temperature-sensitive (ts) mutants were selected that were restricted in capacity to form colonies on blood agar at 38 C. Whereas colony formation by the type I parent (ts+) was unaffected by a temperature of as high as 39 C, the ts mutants exhibited a spectrum of temperature sensitivity in which colony formation was inhibited significantly at 36 C, 37 C, 38 C, or 39 C. Growth of ts mutants at 38 C in broth was reduced or delayed relative to that of ts organisms under identical conditions. In general, there was a direct correlation between degree of temperature sensitivity and genetic stability. Mutants grown at a permissive temperature resembled the ts+ type I parent in colonial morphology and properties of alpha-hemolysis, bile solubility, optochin sensitivity, and antibiotic sensitivity. Moreover, in vitro studies indicated that the mutants retained capsules of immunochemically reactive type I capsular polysaccharide. | [
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