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PMID:19007
|
Activities of some peptidases and glycolytic enzymes in cells of the amniotic fluid. i. Pregnancies terminated prematurely, at term, and postmaturely.
|
Activities of leucylaminopeptidase, gamma-glutamyl transpeptidase, oxytocinase and aldolase were significantly elevated in the cells of amniotic fluids from cases of premature delivery, compared with cases of delivery at term. The authors conclude that examination of the activities of the aforementioned enzymes can be utilized in prenatal diagnosis of the state of maturity of the fetus.
|
Activities of some peptidases and glycolytic enzymes in cells of the amniotic fluid. i. Pregnancies terminated prematurely, at term, and postmaturely. Activities of leucylaminopeptidase, gamma-glutamyl transpeptidase, oxytocinase and aldolase were significantly elevated in the cells of amniotic fluids from cases of premature delivery, compared with cases of delivery at term. The authors conclude that examination of the activities of the aforementioned enzymes can be utilized in prenatal diagnosis of the state of maturity of the fetus.
|
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] |
PMID:19008
|
Variables of the rubella hemagglutination tests employing freeze-dried erythrocytes.
|
The variables which affect the interaction between freeze-dried one-day-old chick erythrocytes and rubella hemagglutinin prepared from rubella-infected porcine kidney cells were defined and evaluated. The sensitivity of the hemagglutination (HA) reaction is much greater at pH 6.0 to 6.2 than at pH 7.0 to 7.5 HEPES (N-2-hydroxyethylpiperazine-N'-2'-ethanesulfonic acid) diluent with added Ca+ or Mg2+ ion gave four- to eightfold higher HA titers than one without divalent cations. The development of agglutinated and non-agglutinated erythrocyte patterns depended much upon the concentrations of gelatin and albumin in the HEPES diluent. Gelatin especially was essential to obtain stable and clearly distinguishable patterns. Optimal conditions for the agglutination of freeze-dried erythrocytes by rubella hemagglutinin were provided when a HEPES-buffered saline at pH 6.2, containing 10(-3) M CaCl2, 0.2 per cent bovine serum albumin, and 0.0025 per cent gelatin was employed throughout as a diluent for serum, hemagglutinin, and freeze-dried erythrocyte suspension. This diluent gave maximally sensitive and reproducible results in rubella HA and hemagglutination-inhibition (HI) tests employing freeze-dried erythrocytes.
|
Variables of the rubella hemagglutination tests employing freeze-dried erythrocytes. The variables which affect the interaction between freeze-dried one-day-old chick erythrocytes and rubella hemagglutinin prepared from rubella-infected porcine kidney cells were defined and evaluated. The sensitivity of the hemagglutination (HA) reaction is much greater at pH 6.0 to 6.2 than at pH 7.0 to 7.5 HEPES (N-2-hydroxyethylpiperazine-N'-2'-ethanesulfonic acid) diluent with added Ca+ or Mg2+ ion gave four- to eightfold higher HA titers than one without divalent cations. The development of agglutinated and non-agglutinated erythrocyte patterns depended much upon the concentrations of gelatin and albumin in the HEPES diluent. Gelatin especially was essential to obtain stable and clearly distinguishable patterns. Optimal conditions for the agglutination of freeze-dried erythrocytes by rubella hemagglutinin were provided when a HEPES-buffered saline at pH 6.2, containing 10(-3) M CaCl2, 0.2 per cent bovine serum albumin, and 0.0025 per cent gelatin was employed throughout as a diluent for serum, hemagglutinin, and freeze-dried erythrocyte suspension. This diluent gave maximally sensitive and reproducible results in rubella HA and hemagglutination-inhibition (HI) tests employing freeze-dried erythrocytes.
|
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] |
PMID:19011
|
Purification of rat liver particulate neutral ribonuclease and comparison of properties with pancreas and serum ribonucleases.
|
Rat liver particulate neutral ribonuclease (EC 3.1.4.22) was extensively purified (up to 40000-fold). It is shown to be an endonuclease, specific for pyrimidine bases, hydrolysing 5'-phosphate ester bonds. The enzyme specificity, Km, pH optimum, stability in acid medium and thermal stability at high temperature are the same as those of rat pancreatic and serum ribonucleases. Like pancreatic and serum neutral ribonucleases, the hepatic enzyme is sensitive to the liver natural inhibitor. This inhibitor was purified 8000-fold; its association with ribonuclease follows zero-order kinetics. These identical properties for ribonuclease of rat liver, pancreas and serum support the hypothesis [Bartholeyns, Peeters-Joris & Baudhuin (1975) Eur. J. Biochem. 60, 385-393] of an extrahepatic origin for the liver enzyme, the plasma ribonuclease of pancreatic origin being taken up by endocytosis in the liver. Neutral ribonuclease activity was detected in all rat organs investigated; its distribution among tissues is different from the distribution of the natural ribonuclear inhibitor.
|
Purification of rat liver particulate neutral ribonuclease and comparison of properties with pancreas and serum ribonucleases. Rat liver particulate neutral ribonuclease (EC 3.1.4.22) was extensively purified (up to 40000-fold). It is shown to be an endonuclease, specific for pyrimidine bases, hydrolysing 5'-phosphate ester bonds. The enzyme specificity, Km, pH optimum, stability in acid medium and thermal stability at high temperature are the same as those of rat pancreatic and serum ribonucleases. Like pancreatic and serum neutral ribonucleases, the hepatic enzyme is sensitive to the liver natural inhibitor. This inhibitor was purified 8000-fold; its association with ribonuclease follows zero-order kinetics. These identical properties for ribonuclease of rat liver, pancreas and serum support the hypothesis [Bartholeyns, Peeters-Joris & Baudhuin (1975) Eur. J. Biochem. 60, 385-393] of an extrahepatic origin for the liver enzyme, the plasma ribonuclease of pancreatic origin being taken up by endocytosis in the liver. Neutral ribonuclease activity was detected in all rat organs investigated; its distribution among tissues is different from the distribution of the natural ribonuclear inhibitor.
|
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-0.007814696058630943,
0.11680782586336136,
-0.01536039263010025
] |
PMID:19012
|
Identification and partial characterization of phospholipases in isolated adrenocortical cells. The effects of synacthen [corticotropin-(1--24)-tetracosapeptide] and calcium ions.
|
Phospholipase A activity was determined in homogenates and subcellular fractions of trypsin-dispersed cat adrenocortical cells. At pH 7.4 homogenate phospholipid hydrolysis was activated by added Ca2+ and inhibited by EGTA. Phospholipid degradation in the presence and absence of Synacthen was completely blocked by EGTA. Ca2+-dependent activation of a membrane-bound phospholipase may be a critical control mechanism for regulating the molecular changes taking place during stimulation by Synacthen.
|
Identification and partial characterization of phospholipases in isolated adrenocortical cells. The effects of synacthen [corticotropin-(1--24)-tetracosapeptide] and calcium ions. Phospholipase A activity was determined in homogenates and subcellular fractions of trypsin-dispersed cat adrenocortical cells. At pH 7.4 homogenate phospholipid hydrolysis was activated by added Ca2+ and inhibited by EGTA. Phospholipid degradation in the presence and absence of Synacthen was completely blocked by EGTA. Ca2+-dependent activation of a membrane-bound phospholipase may be a critical control mechanism for regulating the molecular changes taking place during stimulation by Synacthen.
|
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] |
PMID:19013
|
A pulse-radiolysis study of the manganese-containing superoxide dismutase from Bacillus stearothermophilus.
|
In the preceding paper the mechanism of catalysis of the manganese-containing superoxide dismutase from Bacillus stearothermophilus was shown to involve a 'fast cycle' and a 'slow cycle' [McAdam, Fox, Lavelle & Fielden, 1977 (Biochem. J. 165, 71-79)]. Further properties of the enzyme was considered in the present paper. Pulse-radiolysis studies, under conditions of low substrate concentration to (i.e. when the fast cycle predominates), showed that enzyme activity decreases as pH increases (6.5-10.2). Activity was unaffected by the addition of H2O2 or NaN3 but slightly decreased by KCN. Both H2O2 and the reducing radical anion CO2-- caused a decrease in A480 of the native enzyme. The rate of the fast catalytic cycle was independent of temperature (5-55 degrees C), and as temperature increases the slow cycle becomes relatively more important. Arrhenius parameters of the rate contants were estimated. The possible identity of the various forms of the enzyme is considered.
|
A pulse-radiolysis study of the manganese-containing superoxide dismutase from Bacillus stearothermophilus. In the preceding paper the mechanism of catalysis of the manganese-containing superoxide dismutase from Bacillus stearothermophilus was shown to involve a 'fast cycle' and a 'slow cycle' [McAdam, Fox, Lavelle & Fielden, 1977 (Biochem. J. 165, 71-79)]. Further properties of the enzyme was considered in the present paper. Pulse-radiolysis studies, under conditions of low substrate concentration to (i.e. when the fast cycle predominates), showed that enzyme activity decreases as pH increases (6.5-10.2). Activity was unaffected by the addition of H2O2 or NaN3 but slightly decreased by KCN. Both H2O2 and the reducing radical anion CO2-- caused a decrease in A480 of the native enzyme. The rate of the fast catalytic cycle was independent of temperature (5-55 degrees C), and as temperature increases the slow cycle becomes relatively more important. Arrhenius parameters of the rate contants were estimated. The possible identity of the various forms of the enzyme is considered.
|
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] |
PMID:19014
|
Purification and some properties of arylsulphatases A and B from rabbit kidney cortex.
|
Arylsulphatases A and B (EC 3.1.6.1) of rabbit kidney cortex were purified 5250- and 7720-fold respectively by a multiple-column-chromatography method. The specific activity toward 4-nitrocatechol sulphate was 42mumol/min per mg for arylsulphatase A and 62 mumol/min per mg for arylsulphatase B. Each enzyme migrated as a single band on polyacrylamide-gel electrophoresis, and the enzyme activity corresponded to the band of protein on the gel. The rate of hydrolysis of ascorbic acid 2-sulphate by arylsulphatase A was three times that for cerebroside 3-sulphate. Arylsulphatase B hydrolysed UDP-N--acetylgalactosamine 4-sulphate and glucosamine 4,6-disulphate, but not galactosamine 6-sulphate.
|
Purification and some properties of arylsulphatases A and B from rabbit kidney cortex. Arylsulphatases A and B (EC 3.1.6.1) of rabbit kidney cortex were purified 5250- and 7720-fold respectively by a multiple-column-chromatography method. The specific activity toward 4-nitrocatechol sulphate was 42mumol/min per mg for arylsulphatase A and 62 mumol/min per mg for arylsulphatase B. Each enzyme migrated as a single band on polyacrylamide-gel electrophoresis, and the enzyme activity corresponded to the band of protein on the gel. The rate of hydrolysis of ascorbic acid 2-sulphate by arylsulphatase A was three times that for cerebroside 3-sulphate. Arylsulphatase B hydrolysed UDP-N--acetylgalactosamine 4-sulphate and glucosamine 4,6-disulphate, but not galactosamine 6-sulphate.
|
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] |
PMID:19015
|
Purification and properties of a cellulase from Aspergillus niger.
|
A cellulolytic enzyme was isolated from a commercial cellulase preparation form Aspergillus niger. A yield of about 50mg of enzyme was obtained per 100g of commerial cellulase. The isolated enzyme was homogeneous in the ultracentrifuge at pH 4.0 and 8.0, and in sodium dodecyl sulphate/polyacrylamide-gel electrophoresis but showed one major and two minor bands in disc gel electrophoresis. No carbohydrate was associated with the protein. Amino acid analysis revealed that the enzyme was rich in acidic and aromatic amino acids. Data from the amino acid composition and dodecyl sulphate/polyacrylamide-gel electrophoresis indicated a molecular weight of 26000. The purified enzyme was active towards CM-cellulose, but no activity towards either cellobiose or p-nitrophenyl beta-D-glucoside was detected under the assay conditions used. The pH optimum for the enzyme was pH 3.8-4.0, and it was stable at 25 degrees C over the range pH 1-9; maximum activity (at pH 4.0) was obtained at 45 degrees C. The cellulase was more stable to heat treatment at pH 8.0 than at 4.0. Kinetic studies gave pK values between 4.2 and 5.3 for groups involved in the enzyme-substrate complex.
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Purification and properties of a cellulase from Aspergillus niger. A cellulolytic enzyme was isolated from a commercial cellulase preparation form Aspergillus niger. A yield of about 50mg of enzyme was obtained per 100g of commerial cellulase. The isolated enzyme was homogeneous in the ultracentrifuge at pH 4.0 and 8.0, and in sodium dodecyl sulphate/polyacrylamide-gel electrophoresis but showed one major and two minor bands in disc gel electrophoresis. No carbohydrate was associated with the protein. Amino acid analysis revealed that the enzyme was rich in acidic and aromatic amino acids. Data from the amino acid composition and dodecyl sulphate/polyacrylamide-gel electrophoresis indicated a molecular weight of 26000. The purified enzyme was active towards CM-cellulose, but no activity towards either cellobiose or p-nitrophenyl beta-D-glucoside was detected under the assay conditions used. The pH optimum for the enzyme was pH 3.8-4.0, and it was stable at 25 degrees C over the range pH 1-9; maximum activity (at pH 4.0) was obtained at 45 degrees C. The cellulase was more stable to heat treatment at pH 8.0 than at 4.0. Kinetic studies gave pK values between 4.2 and 5.3 for groups involved in the enzyme-substrate complex.
|
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] |
PMID:19025
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Respiratory effects and amnesia after premedication with morphine or lorazepam.
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Lorazepam, a new benzodiazepine, was compared with morphine for premedication. Ten patients received morphine 10 mg/70 kg i.m. and 10 received lorazepam 4 mg/70 kg i.m. Respiratory effects were assessed from the change in slope (S) and intercept (B) of the carbon dioxide response line, using a development of Read's rebreathing method. Morphine depressed S by 47% (P less than 0.01), but after lorazepam S increased by 27% (P less than 0.05), neither drug altering B significantly. In two volunteers lorazepam was assessed by both the rebreathing and the steady-state methods; after lorazepam S was smaller by the steady-state than by the rebreathing technique. The findings for lorazepam are consistent with the known effects of sleep on carbon dioxide sensitivity. Amnesia lasting 4-8 h occurred in all patients who received lorazepam so that pain and nausea during this period were not recalled, but no patient who received morphine experienced amnesia. We conclude that lorazepam merits further study, particularly where sedation without respiratory depression is needed, as in obstetrics, and where amnesia for uncomfortable procedures is required.
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Respiratory effects and amnesia after premedication with morphine or lorazepam. Lorazepam, a new benzodiazepine, was compared with morphine for premedication. Ten patients received morphine 10 mg/70 kg i.m. and 10 received lorazepam 4 mg/70 kg i.m. Respiratory effects were assessed from the change in slope (S) and intercept (B) of the carbon dioxide response line, using a development of Read's rebreathing method. Morphine depressed S by 47% (P less than 0.01), but after lorazepam S increased by 27% (P less than 0.05), neither drug altering B significantly. In two volunteers lorazepam was assessed by both the rebreathing and the steady-state methods; after lorazepam S was smaller by the steady-state than by the rebreathing technique. The findings for lorazepam are consistent with the known effects of sleep on carbon dioxide sensitivity. Amnesia lasting 4-8 h occurred in all patients who received lorazepam so that pain and nausea during this period were not recalled, but no patient who received morphine experienced amnesia. We conclude that lorazepam merits further study, particularly where sedation without respiratory depression is needed, as in obstetrics, and where amnesia for uncomfortable procedures is required.
|
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] |
PMID:19027
|
Correlation of biochemical data with Apgar scores at birth and at one minute.
|
A prospective study of 66 unselected neonates revealed a better correlation of umbilical artery blood biochemical data with the Apgar score at birth compared with the score at 1 min. The data confirmed also that inclusion of the score for "colour" detracts from the value of the total score. An Apgar score at birth is more valuable than the score at 1 min.
|
Correlation of biochemical data with Apgar scores at birth and at one minute. A prospective study of 66 unselected neonates revealed a better correlation of umbilical artery blood biochemical data with the Apgar score at birth compared with the score at 1 min. The data confirmed also that inclusion of the score for "colour" detracts from the value of the total score. An Apgar score at birth is more valuable than the score at 1 min.
|
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] |
PMID:19028
|
Cancer of the oral cavity, pharynx/larynx and lung in North Thailand: case-control study and analysis of cigar smoke.
|
The unusually high relative frequency of cancer in the laryngeal region in males (18% of all histologically diagnosed cancers) and a sex ratio of unity for lung cancer in Northern Thailand were further explored in a hospital-based case-control study in Chiang Mai. This compared patients having cancers of the oral cavity (including oropharynx), larynx, hypopharynx and lung, with controls in relation to smoking and chewing habits. Statistical analysis indicated that chewing betel is strongly associated with the occurrence of oral cancer in both sexes, and with cancer of the laryngeal region in males. No factors were strongly linked to lung cancer in men, but, in women, urban residence and miang chewing were associated with lung cancer. Analysis of smoke from the two main types of cigars smoked in the region showed that both had high tar content, but there were marked differences in pH. Smoking cigars with alkaline smoke and high tar had an increased risk for laryngeal cancer in males, whereas other cigars with acid smoke and high tar together with manufactured cigarettes had increased risks for lung cancer. These increased risks were not, however, statistically significant.
|
Cancer of the oral cavity, pharynx/larynx and lung in North Thailand: case-control study and analysis of cigar smoke. The unusually high relative frequency of cancer in the laryngeal region in males (18% of all histologically diagnosed cancers) and a sex ratio of unity for lung cancer in Northern Thailand were further explored in a hospital-based case-control study in Chiang Mai. This compared patients having cancers of the oral cavity (including oropharynx), larynx, hypopharynx and lung, with controls in relation to smoking and chewing habits. Statistical analysis indicated that chewing betel is strongly associated with the occurrence of oral cancer in both sexes, and with cancer of the laryngeal region in males. No factors were strongly linked to lung cancer in men, but, in women, urban residence and miang chewing were associated with lung cancer. Analysis of smoke from the two main types of cigars smoked in the region showed that both had high tar content, but there were marked differences in pH. Smoking cigars with alkaline smoke and high tar had an increased risk for laryngeal cancer in males, whereas other cigars with acid smoke and high tar together with manufactured cigarettes had increased risks for lung cancer. These increased risks were not, however, statistically significant.
|
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] |
PMID:19029
|
Blocking factors against leucocyte-dependent melanoma antibody in the sera of melanoma patients.
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Previous studies, using plasmapheresis to remove blocking factors of cell-mediated cytotoxicity to melanoma cells from the circulation of melanoma patients, suggested that leucocyte-dependent antibody to melanoma cells may also be blocked by factors in their sera. The present study confirms these findings, by showing that most patients with disseminated melanoma had melanoma LDA activity in the IgG fraction when this was separated from their sera. This also applied to a high percentage of patients with primary melanoma. Evidence that the blocking factors may be immune complexes was shown by experiments in which LDA activity to melanoma cells was revealed after acidification of melanoma sera to dissociate immune complexes, followed by ultrafiltration through membranes retaining molecules of size greater than 100,000 daltons. Blocking of LDA activity in the retentate recurred when the retentate was recombined with the filtrate. Further studies indicated that the blocking activity showed affinity for the target cell and not the effector cell. Preliminary analysis of the specificity of the blocking suggests that this was similar to that of melanoma antisera. These results appear to show that blocking of LDA activity to melanoma cells is common in melanoma patients and that the assay system may provide a quantitative method for their analysis that may yield information of biological importance in the management of melanoma patients.
|
Blocking factors against leucocyte-dependent melanoma antibody in the sera of melanoma patients. Previous studies, using plasmapheresis to remove blocking factors of cell-mediated cytotoxicity to melanoma cells from the circulation of melanoma patients, suggested that leucocyte-dependent antibody to melanoma cells may also be blocked by factors in their sera. The present study confirms these findings, by showing that most patients with disseminated melanoma had melanoma LDA activity in the IgG fraction when this was separated from their sera. This also applied to a high percentage of patients with primary melanoma. Evidence that the blocking factors may be immune complexes was shown by experiments in which LDA activity to melanoma cells was revealed after acidification of melanoma sera to dissociate immune complexes, followed by ultrafiltration through membranes retaining molecules of size greater than 100,000 daltons. Blocking of LDA activity in the retentate recurred when the retentate was recombined with the filtrate. Further studies indicated that the blocking activity showed affinity for the target cell and not the effector cell. Preliminary analysis of the specificity of the blocking suggests that this was similar to that of melanoma antisera. These results appear to show that blocking of LDA activity to melanoma cells is common in melanoma patients and that the assay system may provide a quantitative method for their analysis that may yield information of biological importance in the management of melanoma patients.
|
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] |
PMID:19030
|
Serum ferritin in haemochromatosis: changes in the isoferritin composition during venesection therapy.
|
The isoferritin composition of serum ferritin in 13 patients with untreated idiopathic haemochromatosis (IHC) has been shown to differ from normal in exhibiting an increase in isoferritins in the pH range 5.54-5.62. A similar change was observed in four patients with gross iron overload secondary to haemolytic anaemia. During the course of venesection therapy there was a progressive rise in isoferritins of pI 5.02-5.06 relative to the more basic isoferritins. These observations are consistent with previous studies showing alterations in tissue isoferritins in untreated IHC before and after venesection therapy and they are compatible with the hypothesis that the more basic isoferritins correspond to a 'storage' ferritin and the more acidic to a 'secretory' ferritin. The studies also provide further evidence for a possible biological role of the individual isoferritins.
|
Serum ferritin in haemochromatosis: changes in the isoferritin composition during venesection therapy. The isoferritin composition of serum ferritin in 13 patients with untreated idiopathic haemochromatosis (IHC) has been shown to differ from normal in exhibiting an increase in isoferritins in the pH range 5.54-5.62. A similar change was observed in four patients with gross iron overload secondary to haemolytic anaemia. During the course of venesection therapy there was a progressive rise in isoferritins of pI 5.02-5.06 relative to the more basic isoferritins. These observations are consistent with previous studies showing alterations in tissue isoferritins in untreated IHC before and after venesection therapy and they are compatible with the hypothesis that the more basic isoferritins correspond to a 'storage' ferritin and the more acidic to a 'secretory' ferritin. The studies also provide further evidence for a possible biological role of the individual isoferritins.
|
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0.005643818061798811,
0.0029784194193780422
] |
PMID:19031
|
Decreased deformability of erythrocytes in haemolytic anaemia associated with glucosephosphate isomerase deficiency.
|
Deformability of erythrocytes from four patients with different types of glucosephosphate isomerase (D-glucose-6-phosphate ketoisomerase, GPI) deficiency has been determined by cell filtration. Young as well as whole erythrocyte populations had a markedly increased rigidity and an abnormally strong attachment of haemoglobin to the inner surface of isolated membranes. Acidic environment may enhance membran rigidity in vitro and also during passage of the erythrocytes through the spleen. The decrease of deformability at a pH of 6.8 was most pronounced in the splenectomized patients, and likewise in erythrocytes from the splenic artery, which were obtained from one patient during splenectomy. It is suggested that the metabolic environment of the spleen, with its low pH, impairs the deformability of GPI-deficient erythrocytes and predisposes them to splenic sequestration. The clinical improvement of all patients following splenectomy which is accompanied by an increase of the erythrocyte survival time and by unchanged reticulocyte counts, is in accordance with this view.
|
Decreased deformability of erythrocytes in haemolytic anaemia associated with glucosephosphate isomerase deficiency. Deformability of erythrocytes from four patients with different types of glucosephosphate isomerase (D-glucose-6-phosphate ketoisomerase, GPI) deficiency has been determined by cell filtration. Young as well as whole erythrocyte populations had a markedly increased rigidity and an abnormally strong attachment of haemoglobin to the inner surface of isolated membranes. Acidic environment may enhance membran rigidity in vitro and also during passage of the erythrocytes through the spleen. The decrease of deformability at a pH of 6.8 was most pronounced in the splenectomized patients, and likewise in erythrocytes from the splenic artery, which were obtained from one patient during splenectomy. It is suggested that the metabolic environment of the spleen, with its low pH, impairs the deformability of GPI-deficient erythrocytes and predisposes them to splenic sequestration. The clinical improvement of all patients following splenectomy which is accompanied by an increase of the erythrocyte survival time and by unchanged reticulocyte counts, is in accordance with this view.
|
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0.03937514126300812,
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] |
PMID:19032
|
A to O bone marrow transplantation in severe aplastic anaemia: dynamics of blood group conversion and demonstration of early dyserythropoiesis in the engrafted marrow.
|
A to O bone marrow transplantation was performed in a 25-year-old male affected with severe aplastic anaemia, the donor being an HLA compatible brother. Three plasma exchanges had to be performed with an Aminco separator to remove the original and recurring anti-A isohaemagglutinins. The dynamics of O to A blood group conversion were followed by means of differential agglutination. An early wave of marked dyserythropoiesis was observed in the engrafted marrow. Mild to moderate GvHD was treated successfully with MTX, bolus high dosage 6-methylprednisolone and, at relapse, with intravenous ALG.
|
A to O bone marrow transplantation in severe aplastic anaemia: dynamics of blood group conversion and demonstration of early dyserythropoiesis in the engrafted marrow. A to O bone marrow transplantation was performed in a 25-year-old male affected with severe aplastic anaemia, the donor being an HLA compatible brother. Three plasma exchanges had to be performed with an Aminco separator to remove the original and recurring anti-A isohaemagglutinins. The dynamics of O to A blood group conversion were followed by means of differential agglutination. An early wave of marked dyserythropoiesis was observed in the engrafted marrow. Mild to moderate GvHD was treated successfully with MTX, bolus high dosage 6-methylprednisolone and, at relapse, with intravenous ALG.
|
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] |
PMID:19033
|
Reciprocal interaction of hemoglobin with oxygen and protons. The influence of allosteric polyanions.
|
The interaction of three inositol esters, inositol hexaphosphate (IHP), inositol pentaphosphate (IPP), and inositol hexasulfate (IHS), with hemoglobin has been investigated. The proton uptake method was used to obtain the six binding constants for deoxy- and oxyhemoglobin. These data combined with oxygen binding curves over a range of cofactor concentrations were used to test theoretical and empirical equations relating the affinity of hemoglobin for oxygen and allosteric effectors. The Bohr and Haldane coefficients in the presence of the inositol esters are unequal at low, but not at high, concentration of the cofactors. The maximum value reached by both parameters increases with the number of negative charges of the polyanion. 2,3-Diphosphoglycerate (DPG) differs sharply from the inositol esters since even at high concentrations of this cofactor, the Haldane coefficient remains elevated. This is a reflection of the negligible affinity of DPG for fully oxygenated hemoglobin.
|
Reciprocal interaction of hemoglobin with oxygen and protons. The influence of allosteric polyanions. The interaction of three inositol esters, inositol hexaphosphate (IHP), inositol pentaphosphate (IPP), and inositol hexasulfate (IHS), with hemoglobin has been investigated. The proton uptake method was used to obtain the six binding constants for deoxy- and oxyhemoglobin. These data combined with oxygen binding curves over a range of cofactor concentrations were used to test theoretical and empirical equations relating the affinity of hemoglobin for oxygen and allosteric effectors. The Bohr and Haldane coefficients in the presence of the inositol esters are unequal at low, but not at high, concentration of the cofactors. The maximum value reached by both parameters increases with the number of negative charges of the polyanion. 2,3-Diphosphoglycerate (DPG) differs sharply from the inositol esters since even at high concentrations of this cofactor, the Haldane coefficient remains elevated. This is a reflection of the negligible affinity of DPG for fully oxygenated hemoglobin.
|
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] |
PMID:19034
|
Conformations of synthetic tetradecapeptide renin substrate and of angiotensin I in aqueous solution.
|
The properties of aqueous solutions of synthetic renin substrate tetradecapeptide (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser) were examined through electrometric titrations, infrared and circular dichroism spectroscopy, and spectrofluorometry. Titration studies of angiotensin I (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu) were also made, whose results indicated a flexible folded conformation similar to that previously proposed for the octapeptide angiotensin II, with a possible additional beta turn at the C terminus. The experimental results of the tetradecapeptide study, associated with Chou and Fasman calculations and with an analysis of structure-activity relationships in renin substrates and competitive inhibitors, led to the proposal of a beta turn involving the His-Pro-Phe-His sequence of the tetradecapeptide. This beta turn would be stabilized by beta-antiparallel interaction between residues 3-4 and 10-12 and by electrostatic attraction between the N-terminal ammonium and C-terminal carboxylate groups and would be destabilized below pH 5 by electrostatic repulsion between His6 and His9. The capacity to assume this conformation is related to structural requirements for renin substrates and competitive inhibitors.
|
Conformations of synthetic tetradecapeptide renin substrate and of angiotensin I in aqueous solution. The properties of aqueous solutions of synthetic renin substrate tetradecapeptide (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser) were examined through electrometric titrations, infrared and circular dichroism spectroscopy, and spectrofluorometry. Titration studies of angiotensin I (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu) were also made, whose results indicated a flexible folded conformation similar to that previously proposed for the octapeptide angiotensin II, with a possible additional beta turn at the C terminus. The experimental results of the tetradecapeptide study, associated with Chou and Fasman calculations and with an analysis of structure-activity relationships in renin substrates and competitive inhibitors, led to the proposal of a beta turn involving the His-Pro-Phe-His sequence of the tetradecapeptide. This beta turn would be stabilized by beta-antiparallel interaction between residues 3-4 and 10-12 and by electrostatic attraction between the N-terminal ammonium and C-terminal carboxylate groups and would be destabilized below pH 5 by electrostatic repulsion between His6 and His9. The capacity to assume this conformation is related to structural requirements for renin substrates and competitive inhibitors.
|
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] |
PMID:19036
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Effects of quaternary ligands on the inhibition of acetylcholinesterase by arsenite.
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Arsenite inhibits acetylcholinesterase in a second-order reaction. The rate and equilibrium constants depend upon pH and have values on the order of 10(2) M-1 min-1 and 10(5) M (dissociation), respectively. Some quaternary ammonium ligands completely block the arsenite inhibition of the enzyme, others decrease the rate of the reaction and some, notably pyridine-2 aldoxime methiodide, greatly accelerate the rate of the reaction, up to 220-fold. Accelerators may bind at a separate enzyme site distinct form the anionic site involved in substrate binding. Although the kinetic data are consistent with a covalent reaction between arsenite and acetylcholinesterase, chemical evidence excludes the involvement of sulfhydryl groups which are usually implicated in arsenite inhibition.
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Effects of quaternary ligands on the inhibition of acetylcholinesterase by arsenite. Arsenite inhibits acetylcholinesterase in a second-order reaction. The rate and equilibrium constants depend upon pH and have values on the order of 10(2) M-1 min-1 and 10(5) M (dissociation), respectively. Some quaternary ammonium ligands completely block the arsenite inhibition of the enzyme, others decrease the rate of the reaction and some, notably pyridine-2 aldoxime methiodide, greatly accelerate the rate of the reaction, up to 220-fold. Accelerators may bind at a separate enzyme site distinct form the anionic site involved in substrate binding. Although the kinetic data are consistent with a covalent reaction between arsenite and acetylcholinesterase, chemical evidence excludes the involvement of sulfhydryl groups which are usually implicated in arsenite inhibition.
|
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] |
PMID:19038
|
Redox properties of microsomal reduced nicotinamide adenine dinucleotide-cytochrome b5 reductase and cytochrome b5.
|
Hepatic NADH-cytochrome b5 reductase was reduced by 1 mol of dithionite or NADH per mol of enzyme-bound FAD, without forming a stable semiquinone or intermediate during the titrations. However, the addition of NAD+ to the partially reduced enzyme or illumination in the presence of both NAD+ and EDTA yielded a new intermediate. The intermediate had an absorption band at 375 nm and the optical spectrum resembled anionic semiquinones seen on reduction of other flavin enzymes. Electron paramagnetic resonance measurements confirmed the free-radical nature of the species. To explain the results, a disproportionation reaction between the oxidized and reduced NAD+ complexes (E-FAD-NAD+ + E-FADH2-NAD+ in equilibrium 2E-FADH.-NAD+) is assumed. Potentiometric titration of NADH-cytochrome b5 reductase at pH 7.0 with dithionite gave a midpoint potential of -258 mV; titration with NADH gave -160 mV. This difference may be due to a difference in the relative affinity of NAD+ for the reduced and oxidized forms of the enzyme. The effects of pH on the midpoint potential of the NAD+-free enzyme were very similar to those which have been measured with free FAD. At pH 7.0, midpoint potentials of trypsin-solubilized and detergent-solubilized cytochrome b5 were 13 and 0 mV, respectively.
|
Redox properties of microsomal reduced nicotinamide adenine dinucleotide-cytochrome b5 reductase and cytochrome b5. Hepatic NADH-cytochrome b5 reductase was reduced by 1 mol of dithionite or NADH per mol of enzyme-bound FAD, without forming a stable semiquinone or intermediate during the titrations. However, the addition of NAD+ to the partially reduced enzyme or illumination in the presence of both NAD+ and EDTA yielded a new intermediate. The intermediate had an absorption band at 375 nm and the optical spectrum resembled anionic semiquinones seen on reduction of other flavin enzymes. Electron paramagnetic resonance measurements confirmed the free-radical nature of the species. To explain the results, a disproportionation reaction between the oxidized and reduced NAD+ complexes (E-FAD-NAD+ + E-FADH2-NAD+ in equilibrium 2E-FADH.-NAD+) is assumed. Potentiometric titration of NADH-cytochrome b5 reductase at pH 7.0 with dithionite gave a midpoint potential of -258 mV; titration with NADH gave -160 mV. This difference may be due to a difference in the relative affinity of NAD+ for the reduced and oxidized forms of the enzyme. The effects of pH on the midpoint potential of the NAD+-free enzyme were very similar to those which have been measured with free FAD. At pH 7.0, midpoint potentials of trypsin-solubilized and detergent-solubilized cytochrome b5 were 13 and 0 mV, respectively.
|
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-0.007050594314932823,
-0.042361870408058167,
-0.035623468458652496,
0.004219158552587032,
0.044411830604076385,
-0.004766062833368778,
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0.006822863593697548,
-0.03321181237697601,
0.05675613135099411,
0.025001417845487595
] |
PMID:19039
|
Phosphoglycerate mutase from wheat germ: studies with isotopically labeled 3-phospho-D-glycerates showing that the catalyzed reaction is intramolecular. Appendix: phosphoglycerate mutase from wheat germ: isolation, crystallization, and properties.
|
The isomerization of 3-phospho-D-glycerate and 2-phospho-D-glycerate catalyzed by the cofactor-independent phosphoglycerate mutase from wheat germ (the isolation and crystallization of which is described in the Appendix) has been shown to be intramolecular by two methods. Mass-spectrometric analysis of the products from the isomerization of a mixture of 3-phospho-D-[2(-2)H]glycerate and 3-[18O]phospho-D-glycerate shows that there is no exchange of labeled phosphoryl group between carbon skeletons in the mutase-catalyzed reaction. Analysis of the products from the isomerization of a mixture of 3-phospho-D-[2(-2)H]glycerate and 3-[32p]phospho-D-glycerate by a method involving the kinetic discrimination between 2(-2)H and 2(-1)H species using the enolase isotope effect similarly shows that the wheat germ phosphoglycerate mutase mediates an intramolecular transfer of the phosphoryl group.
|
Phosphoglycerate mutase from wheat germ: studies with isotopically labeled 3-phospho-D-glycerates showing that the catalyzed reaction is intramolecular. Appendix: phosphoglycerate mutase from wheat germ: isolation, crystallization, and properties. The isomerization of 3-phospho-D-glycerate and 2-phospho-D-glycerate catalyzed by the cofactor-independent phosphoglycerate mutase from wheat germ (the isolation and crystallization of which is described in the Appendix) has been shown to be intramolecular by two methods. Mass-spectrometric analysis of the products from the isomerization of a mixture of 3-phospho-D-[2(-2)H]glycerate and 3-[18O]phospho-D-glycerate shows that there is no exchange of labeled phosphoryl group between carbon skeletons in the mutase-catalyzed reaction. Analysis of the products from the isomerization of a mixture of 3-phospho-D-[2(-2)H]glycerate and 3-[32p]phospho-D-glycerate by a method involving the kinetic discrimination between 2(-2)H and 2(-1)H species using the enolase isotope effect similarly shows that the wheat germ phosphoglycerate mutase mediates an intramolecular transfer of the phosphoryl group.
|
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] |
PMID:19042
|
Preparation and properties of a new DNase from Aspergillus oryzae.
|
A DNase present in commercial preparations of Aspergillus oryzae alpha-amylase was purified 1550-fold in 25% yield by acetone precipitation and by chromatography on diethylaminoethyl- and carboxymethylcellulose. The enzyme was isolated free of contaminating RNases and DNases. The molecular weight of the enzyme determined by gel filtration on Sephadex G-100 was 48 000, while a molecular weight of 58 000 was determined for the single band observed upon polyacrylamide gel electrophoresis in sodium dodecyl sulfate. The isoelectric point of the DNase is 9.2. The enzyme hydrolyzed only DNA with a pH optimum of 8.2 and was activated by Co2+, and to a lesser extent by Mg2+ and Mn2+. Native DNA was a better substrate than heat-denatured DNA. Enzymatic digests of calf thymus and E. coli DNA yielded oligomers of chain lengths ranging from 10 to 200, with mono- and small oligonucleotides (chain length less than 5) detected only when large (100 mg) amounts of DNA were fractionated by column chromatography on diethylaminoethyl-Sephadex A-25 in 7 M urea. The digestion products contained 5'-terminal phosphate groups and mostly adenosine at the 3' and guanosine and adenosine at the 5' ends.
|
Preparation and properties of a new DNase from Aspergillus oryzae. A DNase present in commercial preparations of Aspergillus oryzae alpha-amylase was purified 1550-fold in 25% yield by acetone precipitation and by chromatography on diethylaminoethyl- and carboxymethylcellulose. The enzyme was isolated free of contaminating RNases and DNases. The molecular weight of the enzyme determined by gel filtration on Sephadex G-100 was 48 000, while a molecular weight of 58 000 was determined for the single band observed upon polyacrylamide gel electrophoresis in sodium dodecyl sulfate. The isoelectric point of the DNase is 9.2. The enzyme hydrolyzed only DNA with a pH optimum of 8.2 and was activated by Co2+, and to a lesser extent by Mg2+ and Mn2+. Native DNA was a better substrate than heat-denatured DNA. Enzymatic digests of calf thymus and E. coli DNA yielded oligomers of chain lengths ranging from 10 to 200, with mono- and small oligonucleotides (chain length less than 5) detected only when large (100 mg) amounts of DNA were fractionated by column chromatography on diethylaminoethyl-Sephadex A-25 in 7 M urea. The digestion products contained 5'-terminal phosphate groups and mostly adenosine at the 3' and guanosine and adenosine at the 5' ends.
|
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] |
PMID:19044
|
Structure-function relationships in TPN-dependent isocitrate dehydrogenase. I. Electron paramagnetic resonance studies of the interaction of enzyme-bound Mn(II) with substrates, cofactors, and substrate analogues.
|
Electron paramagnetic resonance (EPR) spectra were obtained for various isocitrate dehydrogenase-Mn(II) complexes. The qualitative effects of the binding of substrates, nucleotides, and substrate analogues on the isotropic character of the electronic environment of enzyme-bound Mn(II) were subsequently investigated. The addition of isocitrate produces a markedly anisotropic spectrum whereas alpha-ketoglutarate does not alter the spectrum of enzyme-Mn(II) substantially. This suggests direct coordination of isocitrate to the Mn(II) but perphaps a different mode of binding for alpha-ketoglutarate. Other studies demonstrated mutually exclusive binding relationships between TPN and TPNH, between Mn-isocitrate and TPNH, and between HCO3-(CO2) and formate or thiocyanate. Indirect evidence supporting CO2 rather than HCO3-as the actual reactive species which binds to the enzyme in the reductive carboxylation reaction is presented on the basis of the results of the formate and thiocyanate studies. From the EPR results recorded for ternary, quaternary, and quinary enzyme-substrate complexes, correlations between the appearance of fine structure signals and the binding of individual substrates and/or nucleotides are found, and tentative assignments of such signals are made on this basis. Additional studies were conducted to determine binding constants for Mg(II) Co(II), and Co-isocitrate, and a comparison was made with kinetically determined binding constants.
|
Structure-function relationships in TPN-dependent isocitrate dehydrogenase. I. Electron paramagnetic resonance studies of the interaction of enzyme-bound Mn(II) with substrates, cofactors, and substrate analogues. Electron paramagnetic resonance (EPR) spectra were obtained for various isocitrate dehydrogenase-Mn(II) complexes. The qualitative effects of the binding of substrates, nucleotides, and substrate analogues on the isotropic character of the electronic environment of enzyme-bound Mn(II) were subsequently investigated. The addition of isocitrate produces a markedly anisotropic spectrum whereas alpha-ketoglutarate does not alter the spectrum of enzyme-Mn(II) substantially. This suggests direct coordination of isocitrate to the Mn(II) but perphaps a different mode of binding for alpha-ketoglutarate. Other studies demonstrated mutually exclusive binding relationships between TPN and TPNH, between Mn-isocitrate and TPNH, and between HCO3-(CO2) and formate or thiocyanate. Indirect evidence supporting CO2 rather than HCO3-as the actual reactive species which binds to the enzyme in the reductive carboxylation reaction is presented on the basis of the results of the formate and thiocyanate studies. From the EPR results recorded for ternary, quaternary, and quinary enzyme-substrate complexes, correlations between the appearance of fine structure signals and the binding of individual substrates and/or nucleotides are found, and tentative assignments of such signals are made on this basis. Additional studies were conducted to determine binding constants for Mg(II) Co(II), and Co-isocitrate, and a comparison was made with kinetically determined binding constants.
|
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] |
PMID:19046
|
Purification and properties of a 3'-phosphoryl former endodeoxyribonuclease from eggs of Asterias forbesi.
|
A DNA endonuclease has been purified from eggs of Asterias forbesi by a simple four-step-purification procedure. The purified enzyme is at least 96% pure and is free of phosphatase, phosphodiesterase, and RNase. It has a pH optimum of 6.5 and does not require divalent cations. The enzyme produces 3'-phosphoryl and 5'-hydroxyl end groups. The products of exhaustive hydrolysis can be grouped in two fractions. The first fraction, 40%, contains a small amount of mononucleotides and di-, tri-, tetra-, penta-, and hexanucleo-tides. The second fraction, 60%, contains oligonucleotides larger than hexanucleotides.
|
Purification and properties of a 3'-phosphoryl former endodeoxyribonuclease from eggs of Asterias forbesi. A DNA endonuclease has been purified from eggs of Asterias forbesi by a simple four-step-purification procedure. The purified enzyme is at least 96% pure and is free of phosphatase, phosphodiesterase, and RNase. It has a pH optimum of 6.5 and does not require divalent cations. The enzyme produces 3'-phosphoryl and 5'-hydroxyl end groups. The products of exhaustive hydrolysis can be grouped in two fractions. The first fraction, 40%, contains a small amount of mononucleotides and di-, tri-, tetra-, penta-, and hexanucleo-tides. The second fraction, 60%, contains oligonucleotides larger than hexanucleotides.
|
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] |
PMID:19047
|
Effect of pH on the interaction of benzoate and D-amino acid oxidase.
|
The kinetic and equilibrium dissociation constants of the reversible binding of benzoate to hog kidney D-amino acid oxidase (DAAO) were studied at 19 degrees C over the pH range 5.3-10.5 by means of a stopped-flow apparatus and spectrophotometric titrations. A simple bimolecular reaction of the form second order-first order was observed; a two-step reaction was seen. Analysis of the pH dependence of the bimolecular rate constants and equilibrium dissociation constants is consistent with three ionizable groups which are important for benzoate binding. The pK values of the enzyme-related ionization are 6.3, 9.2, and 9.6. Analysis of the change in extinction coefficient at 360 nm indicates the pK of 9.6 can be assigned to the 3-imino group of the enzyme-bound flavin. The effect of benzoate on the apparent pK for the ionization of the 3-imino group of the enzyme-bound Fad has been reexamined. The presence of benzoate causes an apparent shift of this ionization from a pK value of 9.6 to 10.7.
|
Effect of pH on the interaction of benzoate and D-amino acid oxidase. The kinetic and equilibrium dissociation constants of the reversible binding of benzoate to hog kidney D-amino acid oxidase (DAAO) were studied at 19 degrees C over the pH range 5.3-10.5 by means of a stopped-flow apparatus and spectrophotometric titrations. A simple bimolecular reaction of the form second order-first order was observed; a two-step reaction was seen. Analysis of the pH dependence of the bimolecular rate constants and equilibrium dissociation constants is consistent with three ionizable groups which are important for benzoate binding. The pK values of the enzyme-related ionization are 6.3, 9.2, and 9.6. Analysis of the change in extinction coefficient at 360 nm indicates the pK of 9.6 can be assigned to the 3-imino group of the enzyme-bound flavin. The effect of benzoate on the apparent pK for the ionization of the 3-imino group of the enzyme-bound Fad has been reexamined. The presence of benzoate causes an apparent shift of this ionization from a pK value of 9.6 to 10.7.
|
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] |
PMID:19053
|
Pre-steady-state kinetics of intermediate formation in the deuteroferriheme-hydrogen peroxide system.
|
The pH dependence of formation of a peroxidatic intermediate from the reaction of deuteroferriheme with hydrogen peroxide has been determined for the region pH 8.7-10.1 from stopped-flow kinetic studies in which absorbancy changes are observed at heme monomer-dimer isosbestic points. Results are interpreted primarily in terms of the attainment of double "steady-state" concentrations of Michaelis-Menten complex I and peroxidatic intermediate I'. A linear correlation of observed first-order rate constants with alpha, the degree of dissociation of heme dimer, has been demonstrated and nonzero intercepts are obtained. Slopes and intercepts show a linear logarithmic dependence on pH which is interpreted in terms of HO2-participation both in the formation and subsequent (catalatic) decomposition of a peroxidatically active intermediate. General acid catalysis of intermediate formation is indicated from studies in phosphate, arsenate, and citrate buffer at pH 7.4-9.3. It is suggested that such catalysis may be responsible for anomalously high rates of H2O2 decomposition previously observed in phosphate buffer solution.
|
Pre-steady-state kinetics of intermediate formation in the deuteroferriheme-hydrogen peroxide system. The pH dependence of formation of a peroxidatic intermediate from the reaction of deuteroferriheme with hydrogen peroxide has been determined for the region pH 8.7-10.1 from stopped-flow kinetic studies in which absorbancy changes are observed at heme monomer-dimer isosbestic points. Results are interpreted primarily in terms of the attainment of double "steady-state" concentrations of Michaelis-Menten complex I and peroxidatic intermediate I'. A linear correlation of observed first-order rate constants with alpha, the degree of dissociation of heme dimer, has been demonstrated and nonzero intercepts are obtained. Slopes and intercepts show a linear logarithmic dependence on pH which is interpreted in terms of HO2-participation both in the formation and subsequent (catalatic) decomposition of a peroxidatically active intermediate. General acid catalysis of intermediate formation is indicated from studies in phosphate, arsenate, and citrate buffer at pH 7.4-9.3. It is suggested that such catalysis may be responsible for anomalously high rates of H2O2 decomposition previously observed in phosphate buffer solution.
|
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0.039872974157333374,
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] |
PMID:19054
|
Escherichia coli dihydrofolate reductase: isolation and characterization of two isozymes.
|
A combination of affinity column chromatography and preparative gel electrophoresis has been used to purify to homogeneity the two isozymes of dihydrofolate reductase from a trimethoprim-resistant strain of Escherichia coli B (RT 500). These enzyme forms are noninterconvertible and are present in crude cell lysates, but other electrophoretic species can be generated durng purification if sulfhydryl-protecting agents, such as dithiothreitol, are not present. The two isozymes, numbered form 1 and form 2 with respect to their decreasing electrophoretic mobilities, have similar molecular weights (18 500), molecular radii (21 A), and apparent Km values for reduced nico inamide adenin- dinucleotide (NADH) and NADH phosphate (NADPH). Both forms contain 2 mol of sulfhydryl/mol of enzyme which can be oxidized to intramolecular disulfide bonds. However, forms 1 and 2 differ physically in their electrophoretic mobility and isoelectric point and kinetically in their pH-activity profile, specific activity, Km for dihydrofolate, and their affinity toward a number of inhibitors.
|
Escherichia coli dihydrofolate reductase: isolation and characterization of two isozymes. A combination of affinity column chromatography and preparative gel electrophoresis has been used to purify to homogeneity the two isozymes of dihydrofolate reductase from a trimethoprim-resistant strain of Escherichia coli B (RT 500). These enzyme forms are noninterconvertible and are present in crude cell lysates, but other electrophoretic species can be generated durng purification if sulfhydryl-protecting agents, such as dithiothreitol, are not present. The two isozymes, numbered form 1 and form 2 with respect to their decreasing electrophoretic mobilities, have similar molecular weights (18 500), molecular radii (21 A), and apparent Km values for reduced nico inamide adenin- dinucleotide (NADH) and NADH phosphate (NADPH). Both forms contain 2 mol of sulfhydryl/mol of enzyme which can be oxidized to intramolecular disulfide bonds. However, forms 1 and 2 differ physically in their electrophoretic mobility and isoelectric point and kinetically in their pH-activity profile, specific activity, Km for dihydrofolate, and their affinity toward a number of inhibitors.
|
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] |
PMID:19055
|
Thermal unfolding transition of ribonuclease A measured by 2'-CMP binding.
|
We report an approach to the problem of detecting and characterising intermediates in the unfolding of ribonuclease A. Two distinct properties of the protein are compared at equilibrium within the unfolding transition zone: (1) a physical property of the protein, the absorbance of buried tyrosine residues, and (2) a functional property, the ability to bind the specific ligand, 2'-CMP. A direct comparison of these two properties is made within the pH 5.8 transition zone, and an indirect comparison is made by using the stopped-flow instrument to sample rapidly the equilibrium properties of the pH 2.0 transition. At both pH 2.0 and pH 5.8, the results indicate that there are no intermediates in folding which have the physical properties of the native enzyme but which have lost the ability to bind a specific ligand.
|
Thermal unfolding transition of ribonuclease A measured by 2'-CMP binding. We report an approach to the problem of detecting and characterising intermediates in the unfolding of ribonuclease A. Two distinct properties of the protein are compared at equilibrium within the unfolding transition zone: (1) a physical property of the protein, the absorbance of buried tyrosine residues, and (2) a functional property, the ability to bind the specific ligand, 2'-CMP. A direct comparison of these two properties is made within the pH 5.8 transition zone, and an indirect comparison is made by using the stopped-flow instrument to sample rapidly the equilibrium properties of the pH 2.0 transition. At both pH 2.0 and pH 5.8, the results indicate that there are no intermediates in folding which have the physical properties of the native enzyme but which have lost the ability to bind a specific ligand.
|
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] |
PMID:19056
|
Partial purification and characterization of an N2-guanine RNA methyltransferase from chicken embryos.
|
An N2-guanine RNA methyltransferase has been purified 1000-fold from chick embryo homogenates by phosphocellulose chromatography followed by chromatography on S-adenosylhomocystein-Sepharose. The enzyme was shown to methylate the G10 position of Escherichia coli B tRNAPhe and has a Km of 3X10(-7) M for tRNAPhe and 1.38 X 10(-6) M for S-adenosylmethionine. The molecular weight was estimated to be 77 000 by gel filtration and the pH optimum was 8.0 to 8.5. Magnesium ion was not required for activity but it stimulated the rate of methylation 1.5-fold with an optimum at 12 mM. Ammonium ion stimulated activity about twofold with an optimum at about 83 mM. Sodium and potassium ions above 0.1 M were inhibitory.
|
Partial purification and characterization of an N2-guanine RNA methyltransferase from chicken embryos. An N2-guanine RNA methyltransferase has been purified 1000-fold from chick embryo homogenates by phosphocellulose chromatography followed by chromatography on S-adenosylhomocystein-Sepharose. The enzyme was shown to methylate the G10 position of Escherichia coli B tRNAPhe and has a Km of 3X10(-7) M for tRNAPhe and 1.38 X 10(-6) M for S-adenosylmethionine. The molecular weight was estimated to be 77 000 by gel filtration and the pH optimum was 8.0 to 8.5. Magnesium ion was not required for activity but it stimulated the rate of methylation 1.5-fold with an optimum at 12 mM. Ammonium ion stimulated activity about twofold with an optimum at about 83 mM. Sodium and potassium ions above 0.1 M were inhibitory.
|
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0.07725299149751663,
-0.0967910960316658,
-0.06030312925577164,
-0.07984606176614761,
0.013035822659730911,
-0.031209375709295273,
-0.013237349689006805,
0.06717193126678467,
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0.09599477052688599,
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] |
PMID:19063
|
Mechanism of pigeon liver malic enzyme modification of histidyl residues by ethoxyformic anhydride.
|
Incubation of malic enzyme (L-malate:NADP+ oxidoreductase (oxaloacetate-decarboxylating), EC 1.1.1.40) with ethoxyformic anhydride caused the time-dependent loss of its ability to catalyze reactions requiring the nucleotide cofactor NADP+ or NADPH, such as the oxidative decarboxylase, the NADP+ - stimualted oxalacetate decarboxylase, the pyruvate reductase, and the pyruvate-medium proton exchange activities. Similar loss of oxidative decarboxylase and pyruvate reductase activities was affected by photo-oxidation in the presence of rose bengal. The inactivation of oxidative decarboxylase activity by ethoxyformic anhydride was accompanied by the reaction of greater than or equal to 2.3 histidyl residues per enzyme site and was strongly inhibited by NADP+. Ethoxyformylation also impaired the ability of malic enzyme to bind NADP+ or NADPH. These results support the involvement of histidyl residue(s) at the nucleotide binding site of malic enzyme.
|
Mechanism of pigeon liver malic enzyme modification of histidyl residues by ethoxyformic anhydride. Incubation of malic enzyme (L-malate:NADP+ oxidoreductase (oxaloacetate-decarboxylating), EC 1.1.1.40) with ethoxyformic anhydride caused the time-dependent loss of its ability to catalyze reactions requiring the nucleotide cofactor NADP+ or NADPH, such as the oxidative decarboxylase, the NADP+ - stimualted oxalacetate decarboxylase, the pyruvate reductase, and the pyruvate-medium proton exchange activities. Similar loss of oxidative decarboxylase and pyruvate reductase activities was affected by photo-oxidation in the presence of rose bengal. The inactivation of oxidative decarboxylase activity by ethoxyformic anhydride was accompanied by the reaction of greater than or equal to 2.3 histidyl residues per enzyme site and was strongly inhibited by NADP+. Ethoxyformylation also impaired the ability of malic enzyme to bind NADP+ or NADPH. These results support the involvement of histidyl residue(s) at the nucleotide binding site of malic enzyme.
|
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] |
PMID:19064
|
Characterization of human platelet UDPglucose-collagen glucosyltransferase using a new rapid assay.
|
A rapid and specific assay has been developed for UDPglucose-collagen glucosyltransferase (UDPglucose: 5-hydroxylysine-collagen glucosyltransferase, EC 2.4.1.66) using galactosylhydroxylysine (Gal-Hyl) as acceptor. Studies with intact human platelets and isolated plasma membranes indicated that about 5--10% of the total activity was surface bound and the rest was of cytoplasmic origin. The two forms of the enzyme had similar broad pH optima (6.5--8.0), Km values for UDPglucose (5 muM) and Gal-Hyl (approx. 4 mM) and for optimal manganese concentrations (25 mM). The soluble form of the enzyme was purified 80-fold. The reaction mechanism was determined as being rapid equilibrium random BiBi + dead end complex or ordered BiBi with UDPglucose being the first substrate to bind. Using Gal-Hyl bound in purified alpha 1 chain of chick skin collagen, a Km value three orders of magnitude less (2 muM) was found than for free Gal-Hyl and the manganese requirement decreased to 2 mM. These results suggest that the binding to the enzyme of Gal-Hyl in the collagen molecule is enhanced by the presence of the protein portion so that the enzyme may be capable of recognizing not only the carbohydrate side chains but also the primary structure of collagen.
|
Characterization of human platelet UDPglucose-collagen glucosyltransferase using a new rapid assay. A rapid and specific assay has been developed for UDPglucose-collagen glucosyltransferase (UDPglucose: 5-hydroxylysine-collagen glucosyltransferase, EC 2.4.1.66) using galactosylhydroxylysine (Gal-Hyl) as acceptor. Studies with intact human platelets and isolated plasma membranes indicated that about 5--10% of the total activity was surface bound and the rest was of cytoplasmic origin. The two forms of the enzyme had similar broad pH optima (6.5--8.0), Km values for UDPglucose (5 muM) and Gal-Hyl (approx. 4 mM) and for optimal manganese concentrations (25 mM). The soluble form of the enzyme was purified 80-fold. The reaction mechanism was determined as being rapid equilibrium random BiBi + dead end complex or ordered BiBi with UDPglucose being the first substrate to bind. Using Gal-Hyl bound in purified alpha 1 chain of chick skin collagen, a Km value three orders of magnitude less (2 muM) was found than for free Gal-Hyl and the manganese requirement decreased to 2 mM. These results suggest that the binding to the enzyme of Gal-Hyl in the collagen molecule is enhanced by the presence of the protein portion so that the enzyme may be capable of recognizing not only the carbohydrate side chains but also the primary structure of collagen.
|
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] |
PMID:19066
|
Cyclic AMP-dependent protein kinase phosphorylation of cardiac (Na+ + K+)-ATPases. Effect on calcium binding.
|
1. Calcium binding to (Na+ + K+)-ATPase (ATP phosphohydrolase, EC 3.6.1.3) preparations from beef and pig heart preparations of varying degrees of purity was measured. 2. Binding was inhibited by Mg2+, Na+ and K+. Inhibition by Na+ and K+ appeared to be due to an ionic strength effect. 3. Four classes of binding sites were identified with Kd values for calcium of about 0.03, 1, 15 and 200 micrometer. 4. Cyclic AMP-dependent phosphorylation of the enzyme by protein kinase (ATP: protamine O-phosphotransferase, EC 2.7.1.70) had no effect on (Na+ + K+)-ATPase activity. 5. Phosphorylation also had no effect on either Kd or Bmax for calcium binding at any of the four sites whether measured in the presence of absence of NaCl or KCl. 6. It is concluded that previous reports of an effect of phosphorylation on calcium binding to a (Na+ + K+)-ATPase preparation may have been due to the presence of membrane material not directly associated with (Na+ + K+)-ATPase.
|
Cyclic AMP-dependent protein kinase phosphorylation of cardiac (Na+ + K+)-ATPases. Effect on calcium binding. 1. Calcium binding to (Na+ + K+)-ATPase (ATP phosphohydrolase, EC 3.6.1.3) preparations from beef and pig heart preparations of varying degrees of purity was measured. 2. Binding was inhibited by Mg2+, Na+ and K+. Inhibition by Na+ and K+ appeared to be due to an ionic strength effect. 3. Four classes of binding sites were identified with Kd values for calcium of about 0.03, 1, 15 and 200 micrometer. 4. Cyclic AMP-dependent phosphorylation of the enzyme by protein kinase (ATP: protamine O-phosphotransferase, EC 2.7.1.70) had no effect on (Na+ + K+)-ATPase activity. 5. Phosphorylation also had no effect on either Kd or Bmax for calcium binding at any of the four sites whether measured in the presence of absence of NaCl or KCl. 6. It is concluded that previous reports of an effect of phosphorylation on calcium binding to a (Na+ + K+)-ATPase preparation may have been due to the presence of membrane material not directly associated with (Na+ + K+)-ATPase.
|
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] |
PMID:19067
|
3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase. An optimized assay in homogenates of developing brain.
|
An optimized in vitro assay of 3'-phosphoadenylysulfate:galactosylceramide 3'-sulfotransferase (EC 2.8.2.11, galactosylceramide sulfotransferase, formerly known as galactocerebroside sulfotransferase) activity is presented, that can be used in crude homogenate of brain tissue of various developmental stages. The enzyme activity is determined by measuring the [35S]sulfatides formed by the enzymic transfer of [35S]sulfate from 3'-phosphoadenoside 5'-phospho [35S]sulfate to galactosylceramides. The sulfatide formation at 30 degrees C is linear up to 30 min and up to a protein concentration of 1 mg per 0.5 ml assay volume. The presence of 0.4% Triton X-100 and 50 micrometer exogenous bovine cerebrosides are optimal for enzyme activity. The pH optimum of the reaction is at pH 6.5 using 0.1 M imidazole buffer. The enzyme reaction is stimulated by NaCl, KCl, MgCl2, CaCl2, MnCl2, ATP and inhibited by ADP. The developmental enzyme activity pattern of mouse brain is the same, if derived from homogenates and microsomes, respectively, under our assay conditions.
|
3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase. An optimized assay in homogenates of developing brain. An optimized in vitro assay of 3'-phosphoadenylysulfate:galactosylceramide 3'-sulfotransferase (EC 2.8.2.11, galactosylceramide sulfotransferase, formerly known as galactocerebroside sulfotransferase) activity is presented, that can be used in crude homogenate of brain tissue of various developmental stages. The enzyme activity is determined by measuring the [35S]sulfatides formed by the enzymic transfer of [35S]sulfate from 3'-phosphoadenoside 5'-phospho [35S]sulfate to galactosylceramides. The sulfatide formation at 30 degrees C is linear up to 30 min and up to a protein concentration of 1 mg per 0.5 ml assay volume. The presence of 0.4% Triton X-100 and 50 micrometer exogenous bovine cerebrosides are optimal for enzyme activity. The pH optimum of the reaction is at pH 6.5 using 0.1 M imidazole buffer. The enzyme reaction is stimulated by NaCl, KCl, MgCl2, CaCl2, MnCl2, ATP and inhibited by ADP. The developmental enzyme activity pattern of mouse brain is the same, if derived from homogenates and microsomes, respectively, under our assay conditions.
|
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] |
PMID:19068
|
Spontaneous reactivation of acetylcholinesterase following organophosphate inhibition. I. An analysis of anomalous reactivation kinetics.
|
The first kinetic studies on the spontaneous reactivation of Sarin-inhibited acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) are reported. With increasing pH the extent of reactivation increases while the observed rate constant decreases. An analysis of the change in aging rate constant as a function of pH suggests that the aging of alkyl-alkoxy phosphonylated acetylcholinesterases is not solely acid catalyzed.
|
Spontaneous reactivation of acetylcholinesterase following organophosphate inhibition. I. An analysis of anomalous reactivation kinetics. The first kinetic studies on the spontaneous reactivation of Sarin-inhibited acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) are reported. With increasing pH the extent of reactivation increases while the observed rate constant decreases. An analysis of the change in aging rate constant as a function of pH suggests that the aging of alkyl-alkoxy phosphonylated acetylcholinesterases is not solely acid catalyzed.
|
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] |
PMID:19069
|
Comparative studies on immobilization of human prostatic acid phosphatase.
|
Acid phosphatase (othophosphoric monoester phosphohydrolase (acid optimum), EC 3.1.3.2) from the human prostate was immobilized by its protein moiety on cyanogen bromide-activated Sepharose, by carbohydrate moiety on Concanavalin-A-Sepharose, and by Schiff base formation with partially oxidized carbohydrate groups on ethylenediamine-Sepharose. The highest retention of enzyme activity, 80%, was found for the noncovalent immobilization on Concanavalin-A-Sepharose. It was demonstrated that the optimal pH changes for the Concanavalin-A-Sepharose and CNBr-Sepharose-enzyme complexes are electrostratic in character. In all cases of immobilization the enzyme has higher thermostability than that for the native enzyme under the same conditions. The effects of the enzyme stabilization were interpreted in terms of the multipoint interaction between the enzyme molecule and the carrier.
|
Comparative studies on immobilization of human prostatic acid phosphatase. Acid phosphatase (othophosphoric monoester phosphohydrolase (acid optimum), EC 3.1.3.2) from the human prostate was immobilized by its protein moiety on cyanogen bromide-activated Sepharose, by carbohydrate moiety on Concanavalin-A-Sepharose, and by Schiff base formation with partially oxidized carbohydrate groups on ethylenediamine-Sepharose. The highest retention of enzyme activity, 80%, was found for the noncovalent immobilization on Concanavalin-A-Sepharose. It was demonstrated that the optimal pH changes for the Concanavalin-A-Sepharose and CNBr-Sepharose-enzyme complexes are electrostratic in character. In all cases of immobilization the enzyme has higher thermostability than that for the native enzyme under the same conditions. The effects of the enzyme stabilization were interpreted in terms of the multipoint interaction between the enzyme molecule and the carrier.
|
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-0.08096754550933838,
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] |
PMID:19070
|
Harmaline interaction with sodium-binding sites in intestinal brush border sucrase.
|
The effect of harmaline on rabbit brush border sucrase has been studied at pH 6.8. An initial analysis in classical kinetic terms revealed harmaline to be a fully competitive inhibitor of the substrate, sucrose. In spite of this result however, the following hypothesis has been tested. Harmaline, which is positively charged in the physiological range of pH, might in fact compete, not directly with the substrate site, but rather with an allosterically-related sodium-binding site which has been postulated to be involved in the activation of sucrase by the alkali-metal ions (Mahmood and Alvarado, Arch. Biochem. Biophys. 168, 585, 1975). Because of its size, harmaline, when bound to the metal site, could at least partially overlap with the substrate site, thereby behaving as if it were an authentic fully competitive inhibitor of the substrate. This hypothesis appears to be confirmed by the fact that the alkali metals can completely reverse the inhibition caused by harmaline.
|
Harmaline interaction with sodium-binding sites in intestinal brush border sucrase. The effect of harmaline on rabbit brush border sucrase has been studied at pH 6.8. An initial analysis in classical kinetic terms revealed harmaline to be a fully competitive inhibitor of the substrate, sucrose. In spite of this result however, the following hypothesis has been tested. Harmaline, which is positively charged in the physiological range of pH, might in fact compete, not directly with the substrate site, but rather with an allosterically-related sodium-binding site which has been postulated to be involved in the activation of sucrase by the alkali-metal ions (Mahmood and Alvarado, Arch. Biochem. Biophys. 168, 585, 1975). Because of its size, harmaline, when bound to the metal site, could at least partially overlap with the substrate site, thereby behaving as if it were an authentic fully competitive inhibitor of the substrate. This hypothesis appears to be confirmed by the fact that the alkali metals can completely reverse the inhibition caused by harmaline.
|
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] |
PMID:19071
|
Purification of angiotensin I-converting enzyme from human lung.
|
Angiotensin I-converting enzyme (peptidyl dipeptide hydrolase, EC 3.4.15.1) was solubilized from the membrane fraction of human lung using trypsin treatment and purfied using columns of DE 52-cellulose, hydroxyapatite and Sephadex G-200. The purified enzyme was shown to convert angiotensin I to angiotensin II and also to inactivate bradykinin. The specific activity of the enzyme was 9.5 units/mg protein for Hippuryl-His-Leu-OH and 0.665 mumol/min per mg protein for angiotensin I. The enzymic activity obtained after trypsin treatment (1 mg/200 mg protein) for 2 h could be divided into three components: (i) an enzyme of molecular weight 290 000 (peak I), (ii) an enzyme of molecular weight 180 000 (peak II) and (iii) an enzyme of molecular weight 98 000 (peak III), by columns of DE 52-cellulose and Sephadex G-200. Km values of peak I, II and III fraction for Hippuryl-His-Leu-OH were identical at 1.1 mM. pH optimum of the enzyme was 8.3 for Hippuryl-His-Leu-OH.
|
Purification of angiotensin I-converting enzyme from human lung. Angiotensin I-converting enzyme (peptidyl dipeptide hydrolase, EC 3.4.15.1) was solubilized from the membrane fraction of human lung using trypsin treatment and purfied using columns of DE 52-cellulose, hydroxyapatite and Sephadex G-200. The purified enzyme was shown to convert angiotensin I to angiotensin II and also to inactivate bradykinin. The specific activity of the enzyme was 9.5 units/mg protein for Hippuryl-His-Leu-OH and 0.665 mumol/min per mg protein for angiotensin I. The enzymic activity obtained after trypsin treatment (1 mg/200 mg protein) for 2 h could be divided into three components: (i) an enzyme of molecular weight 290 000 (peak I), (ii) an enzyme of molecular weight 180 000 (peak II) and (iii) an enzyme of molecular weight 98 000 (peak III), by columns of DE 52-cellulose and Sephadex G-200. Km values of peak I, II and III fraction for Hippuryl-His-Leu-OH were identical at 1.1 mM. pH optimum of the enzyme was 8.3 for Hippuryl-His-Leu-OH.
|
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] |
PMID:19072
|
Isolation of buffalo muscle aldolase and comparison of its properties with those of rabbit muscle aldolase .
|
Fructose-1,6-bisphosphate aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phyosphate-lyase, EC 4.1.2.13) was isolated from buffalo muscle by fractionation with ammonium sulphate and subsequent purification by phosphocellulose column chromatography using a linear salt gradient. As judged by gel filtration and electrophoresis in polyacrylamide gel, the enzyme was homogeneous with respect to size and charge. The molecular weight and Stokes radius of the enzyme were determined from its elution profile on a calibrated Sephadex column and the respective values were 162000 and 4.55 nm. The diffusion coefficient and frictional ratio were computed to be 4.8-10(7) cm2-s-1 and 1.27, respectively. The molecular weight of the polypeptide chain as measured by aodium dodecyl sulphate polyacrylamide gel electrophoresis was 40750. This taken together with the native molecular weight suggested a four-subunit model for the protein. The N- AND C-terminal residues of polypeptide chains were identified to be proline and tyrosine, respectively. At pH 8.0 the Michaelis-Menten constant and maximum attainable velocity were found to be 8.1 muM and 27 muM Fru-1,6-P2 split/min per mg, respectively. The buffalo muscle aldolase was found to be similar to rabbit muscle aldolase in physico-chemical properties. However, the two enzymes differ significantly in pH optimum; the p optima of the buffalo and rabbit enzymes were determined under identical conditions to be 8.0 and 8.6, respectively.
|
Isolation of buffalo muscle aldolase and comparison of its properties with those of rabbit muscle aldolase . Fructose-1,6-bisphosphate aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phyosphate-lyase, EC 4.1.2.13) was isolated from buffalo muscle by fractionation with ammonium sulphate and subsequent purification by phosphocellulose column chromatography using a linear salt gradient. As judged by gel filtration and electrophoresis in polyacrylamide gel, the enzyme was homogeneous with respect to size and charge. The molecular weight and Stokes radius of the enzyme were determined from its elution profile on a calibrated Sephadex column and the respective values were 162000 and 4.55 nm. The diffusion coefficient and frictional ratio were computed to be 4.8-10(7) cm2-s-1 and 1.27, respectively. The molecular weight of the polypeptide chain as measured by aodium dodecyl sulphate polyacrylamide gel electrophoresis was 40750. This taken together with the native molecular weight suggested a four-subunit model for the protein. The N- AND C-terminal residues of polypeptide chains were identified to be proline and tyrosine, respectively. At pH 8.0 the Michaelis-Menten constant and maximum attainable velocity were found to be 8.1 muM and 27 muM Fru-1,6-P2 split/min per mg, respectively. The buffalo muscle aldolase was found to be similar to rabbit muscle aldolase in physico-chemical properties. However, the two enzymes differ significantly in pH optimum; the p optima of the buffalo and rabbit enzymes were determined under identical conditions to be 8.0 and 8.6, respectively.
|
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] |
PMID:19074
|
Purification of methylmalonyl-CoA mutase from Propionibacterium shermanii using affinity chromatography.
|
A novel procedure for the purification of methylmalonyl-CA mutase from Propionibacterium shermanii has been described which employs affinity chromatography on a column of immobilized vitamin B-12 linked covalently to Sepharose. The method has the advantage of being simple and rapid, thus enabling the purification of the enzyme to near homogeneity with good yields.
|
Purification of methylmalonyl-CoA mutase from Propionibacterium shermanii using affinity chromatography. A novel procedure for the purification of methylmalonyl-CA mutase from Propionibacterium shermanii has been described which employs affinity chromatography on a column of immobilized vitamin B-12 linked covalently to Sepharose. The method has the advantage of being simple and rapid, thus enabling the purification of the enzyme to near homogeneity with good yields.
|
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] |
PMID:19075
|
Enhanced heat, alkaline and tryptic stability of acetamidinated pig heart lactate dehydrogenase.
|
Modification of 17 from 24 lysine residues in pig heart lactate dehydrogenase (L-lactate: NAD+ oxidoreductase, EC 1.1.1.27) with methyl aceimidate yields an enzyme derivative with enhanced stability toward meat and alkaline denaturation as well as tryptic digestion. The specific activity of the modified enzyme is only slightly reduced
|
Enhanced heat, alkaline and tryptic stability of acetamidinated pig heart lactate dehydrogenase. Modification of 17 from 24 lysine residues in pig heart lactate dehydrogenase (L-lactate: NAD+ oxidoreductase, EC 1.1.1.27) with methyl aceimidate yields an enzyme derivative with enhanced stability toward meat and alkaline denaturation as well as tryptic digestion. The specific activity of the modified enzyme is only slightly reduced
|
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] |
PMID:19076
|
Solubilization and partial characterization of UDP-N-acetylgalactosamine: globoside alpha-N-acetylgalactosaminyltransferase from dog spleen microsomes.
|
UDP-N-acetylgalactosamine:globoside alpha-N-acetylgalactosaminyltransferase (EC 2.4.1.-) synthesizing Forssman hapten was solubilized from dog spleen microsomes by a combination of Triton X-100 treatment and sonication. The solubilized enzyme was partially purified by calcium phosphate gel, ammonium sulfate fractionation and then DEAE-cellulose column chromatography. The enzymatic activity of the purified preparation was stimulated by exogenously added phosphatidylserine, as found in the particulate enzyme. When the properties of the purified enzyme were examined in the presence of exogenous phosphatidylserine, the enzyme had an absolute requirement for Mn2+; this was not substituted by Ca2+ or Mg2+. Apparent Km values for UDP-N-acetylgalactosamine and globoside were 1-10(-5) and 5-10(-4) M, respectively. It had a pH optimum of 6.55 regardless of the presence or absence of exogenous lipids. Since the partially purified enzyme was completely free of uridine diphosphatase which was found in the particulate preparaton, the effect of UDP on the transferase activity could be studied. Thus, UDP inhibited 85% of the activity at a concentration of 1.5 mM. p-Cholormercuribenzoate inhibited over 90% of the activity at 2 mM, indicating the transferase to be SH-enzyme.
|
Solubilization and partial characterization of UDP-N-acetylgalactosamine: globoside alpha-N-acetylgalactosaminyltransferase from dog spleen microsomes. UDP-N-acetylgalactosamine:globoside alpha-N-acetylgalactosaminyltransferase (EC 2.4.1.-) synthesizing Forssman hapten was solubilized from dog spleen microsomes by a combination of Triton X-100 treatment and sonication. The solubilized enzyme was partially purified by calcium phosphate gel, ammonium sulfate fractionation and then DEAE-cellulose column chromatography. The enzymatic activity of the purified preparation was stimulated by exogenously added phosphatidylserine, as found in the particulate enzyme. When the properties of the purified enzyme were examined in the presence of exogenous phosphatidylserine, the enzyme had an absolute requirement for Mn2+; this was not substituted by Ca2+ or Mg2+. Apparent Km values for UDP-N-acetylgalactosamine and globoside were 1-10(-5) and 5-10(-4) M, respectively. It had a pH optimum of 6.55 regardless of the presence or absence of exogenous lipids. Since the partially purified enzyme was completely free of uridine diphosphatase which was found in the particulate preparaton, the effect of UDP on the transferase activity could be studied. Thus, UDP inhibited 85% of the activity at a concentration of 1.5 mM. p-Cholormercuribenzoate inhibited over 90% of the activity at 2 mM, indicating the transferase to be SH-enzyme.
|
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-0.031394775956869125,
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-0.012563107535243034,
-0.08069596439599991,
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-0.05204508826136589,
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] |
PMID:19077
|
A conformational change in phosphoglycerate dehydrogenase induced by a shift in pH.
|
The fluorescence of NADH bound to phosphoglycerate dehydrogenase (3-phosphoglycerate: NAD+ oxidoreductase, EC 1.1.1.95) decreased by 42% between pH 8.5 and 7.0 Serine, an allosteric inhibitor, quenched the fluorescence of enzyme-bound NADH by 29% at pH 8.5, but not at all at pH 7.0. The kinetics of the fluorescence change which occurred when the pH of an enzyme-NADH solution was rapidly shifted from 8.5 to 7.0 was measured using stopped-flow fluorimetry. The kinetics were first order, with a rate constant of 2.83 s-1. This rate constant was similar in magnitude to the rate constants for fluorescence quenching at pH 8.5 by saturating concentrations of serine and glycine, another allosteric inhibitor (Dubrow, R. and Pizer, L.I. (1977) J. Biol. Chem. 252, 1527-1538). These results indicate that the conformation of phosphoglycerate dehydrogenase at pH 7.0 is similar to, but not identical with, the serine-induced conformation at pH 8.5.
|
A conformational change in phosphoglycerate dehydrogenase induced by a shift in pH. The fluorescence of NADH bound to phosphoglycerate dehydrogenase (3-phosphoglycerate: NAD+ oxidoreductase, EC 1.1.1.95) decreased by 42% between pH 8.5 and 7.0 Serine, an allosteric inhibitor, quenched the fluorescence of enzyme-bound NADH by 29% at pH 8.5, but not at all at pH 7.0. The kinetics of the fluorescence change which occurred when the pH of an enzyme-NADH solution was rapidly shifted from 8.5 to 7.0 was measured using stopped-flow fluorimetry. The kinetics were first order, with a rate constant of 2.83 s-1. This rate constant was similar in magnitude to the rate constants for fluorescence quenching at pH 8.5 by saturating concentrations of serine and glycine, another allosteric inhibitor (Dubrow, R. and Pizer, L.I. (1977) J. Biol. Chem. 252, 1527-1538). These results indicate that the conformation of phosphoglycerate dehydrogenase at pH 7.0 is similar to, but not identical with, the serine-induced conformation at pH 8.5.
|
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] |
PMID:19080
|
Ganglioside biosynthesis. Characterization of CMP-N-acetylneuraminic acid : lactosylceramide sialyltransferase in Golgi apparatus from rat liver.
|
An enzyme that transfers sialic acid from GMP-sialic acid to lactosylceramide was concentrated 40-50 times in Golgi apparatus from rat liver relative to total homogenates. This enzyme required detergents as dispersing agents. Of the numerous detergents tested, the combination Tween 80-Triton CF-54 (1 : 2, w/w) was the most effective in stimulating the reaction. Two apparent pH optima, at 6.35 and 5.5, were observed. The enzyme showed no requirement for a divalent cation. The Km values calculated for CMP-N-acetylneuraminic acid and lactosylceramide were 2.7 - 10(-3) and 1.3 - 10(-4) M, respectively. The enzyme could not be dissociated from Golgi apparatus fractions by treatment with ultrasound, indicating that it is tightly associated with the membrane. The newly synthesized GM3, the product of the reaction, was incorporated into or became tightly associated with the membranes of the Golgi apparatus.
|
Ganglioside biosynthesis. Characterization of CMP-N-acetylneuraminic acid : lactosylceramide sialyltransferase in Golgi apparatus from rat liver. An enzyme that transfers sialic acid from GMP-sialic acid to lactosylceramide was concentrated 40-50 times in Golgi apparatus from rat liver relative to total homogenates. This enzyme required detergents as dispersing agents. Of the numerous detergents tested, the combination Tween 80-Triton CF-54 (1 : 2, w/w) was the most effective in stimulating the reaction. Two apparent pH optima, at 6.35 and 5.5, were observed. The enzyme showed no requirement for a divalent cation. The Km values calculated for CMP-N-acetylneuraminic acid and lactosylceramide were 2.7 - 10(-3) and 1.3 - 10(-4) M, respectively. The enzyme could not be dissociated from Golgi apparatus fractions by treatment with ultrasound, indicating that it is tightly associated with the membrane. The newly synthesized GM3, the product of the reaction, was incorporated into or became tightly associated with the membranes of the Golgi apparatus.
|
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] |
PMID:19081
|
Thermodynamics of lipid protein associations. Thermodynamics of helix formation in the association of high density apolipoprotein A-I (apoA-I) to dimyristoyl phosphatidylcholine.
|
The structure and phospholipid-binding properties of human plasma high density apolipoprotein A-I (apoA-I) has been studied at pH 7.4 and 3.1 by microcalorimetry, circular dichroism and density gradient ultracentrifugation. At pH values of 7.4 and 3.1, apoA-I binds to dimyristoyl phosphatidylcholine (DMPC) to form complexes of similar composition (molar ratio of DMPC/apoA-I of 100) and helical content (67%). At pH 7.4, the lipid-protein association is accompanied by an increase in helical content from 58 to 67% and an exothermic enthalpy of binding (deltaHB) of -90 kcal/mol apoA-I. At pH 3.1, the helical content of apoA-I is increased from 48 to 67% on binding to DMPC and the enthalpy of binding was -170 kcal/mol. We suggest that the difference in the enthalpies of binding (-80 kcal/mol) at pH 3.1 compared to 7.4 is due to the greater coil leads to helix transition at the lower pH.
|
Thermodynamics of lipid protein associations. Thermodynamics of helix formation in the association of high density apolipoprotein A-I (apoA-I) to dimyristoyl phosphatidylcholine. The structure and phospholipid-binding properties of human plasma high density apolipoprotein A-I (apoA-I) has been studied at pH 7.4 and 3.1 by microcalorimetry, circular dichroism and density gradient ultracentrifugation. At pH values of 7.4 and 3.1, apoA-I binds to dimyristoyl phosphatidylcholine (DMPC) to form complexes of similar composition (molar ratio of DMPC/apoA-I of 100) and helical content (67%). At pH 7.4, the lipid-protein association is accompanied by an increase in helical content from 58 to 67% and an exothermic enthalpy of binding (deltaHB) of -90 kcal/mol apoA-I. At pH 3.1, the helical content of apoA-I is increased from 48 to 67% on binding to DMPC and the enthalpy of binding was -170 kcal/mol. We suggest that the difference in the enthalpies of binding (-80 kcal/mol) at pH 3.1 compared to 7.4 is due to the greater coil leads to helix transition at the lower pH.
|
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0.05279817059636116,
0.05612565577030182,
-0.0100856339558959,
-0.06282664090394974,
-0.0009190397104248405,
0.05151742696762085,
0.10340876877307892,
0.012880226597189903,
-0.06721683591604233,
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] |
PMID:19082
|
Characterization and partial purification of acid lipase from human leucocytes.
|
Hydrolysis of glycerol trioleate by human leucocytes was characterized and the enzymes responsible for this activity were obtained in a purified form by means of gel chromatography on Sephadex G-100 as well as by zonal ultracentrifugation followed by gel chromatography. The activity is localized in the granule fraction of leucocytes (15 000 X g, 20 min) and shows a sharp pH optimum at pH 5.25. As judged from the elution profile obtained by gel chromatography, two proteins are likely to contribute to the hydrolysis of glycerol trioleate. The approximate molecular weights of the two enzymes are 74 100 and 60 300, respectively. The activity is reduced in the presence of NaCl, KCl, CaCl2 as well as of p-hydroxymercuribenzoate. The enzymes are stable at -25 degrees C but loose about 50% of their activity within 48 h at 4 degrees C.
|
Characterization and partial purification of acid lipase from human leucocytes. Hydrolysis of glycerol trioleate by human leucocytes was characterized and the enzymes responsible for this activity were obtained in a purified form by means of gel chromatography on Sephadex G-100 as well as by zonal ultracentrifugation followed by gel chromatography. The activity is localized in the granule fraction of leucocytes (15 000 X g, 20 min) and shows a sharp pH optimum at pH 5.25. As judged from the elution profile obtained by gel chromatography, two proteins are likely to contribute to the hydrolysis of glycerol trioleate. The approximate molecular weights of the two enzymes are 74 100 and 60 300, respectively. The activity is reduced in the presence of NaCl, KCl, CaCl2 as well as of p-hydroxymercuribenzoate. The enzymes are stable at -25 degrees C but loose about 50% of their activity within 48 h at 4 degrees C.
|
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] |
PMID:19083
|
The isolation and characterization of sphingomyelinase from human placental tissue.
|
Human placental sphingomyelinase activity was eluted as a single symmetrical peak from Sephadex G-200 with a molecular weight of 290000; however, the enzyme behaved heterogeneously on ion exchange chromatography. A specific species of sphingomyelinase was purified approx. 10 000-fold to a constant specific activity of 274 000 nanomol of sphingomyelin hydrolyzed per mg protein per h. When the purified enzyme was examined on sodium dodecyl sulfate disc gel electrophoresis, two distinct protein bands in approximately equal proportions with molecular weights of 36 800 and 28 300 were found. The specificity of the enzyme is directed towards both the hydrophilic phosphocholine and the hydrophobic ceramide moieties of sphingomyelin. Possible interrelationships between the heterogenous forms of placental sphingomyelinases are discussed.
|
The isolation and characterization of sphingomyelinase from human placental tissue. Human placental sphingomyelinase activity was eluted as a single symmetrical peak from Sephadex G-200 with a molecular weight of 290000; however, the enzyme behaved heterogeneously on ion exchange chromatography. A specific species of sphingomyelinase was purified approx. 10 000-fold to a constant specific activity of 274 000 nanomol of sphingomyelin hydrolyzed per mg protein per h. When the purified enzyme was examined on sodium dodecyl sulfate disc gel electrophoresis, two distinct protein bands in approximately equal proportions with molecular weights of 36 800 and 28 300 were found. The specificity of the enzyme is directed towards both the hydrophilic phosphocholine and the hydrophobic ceramide moieties of sphingomyelin. Possible interrelationships between the heterogenous forms of placental sphingomyelinases are discussed.
|
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] |
PMID:19084
|
Reaction of selenium with immunoglobulin molecules.
|
Radioactive selenite reacts with purified human and goat immunoglobulins at acidic and neutral pH. The antigenic properties of the immunoglobulins are retained during the selenium labelling as shown by immunoelectrophoresis and autoradiography. Pepsin digests of 75Se-labelled IgG possess 75Se both in the (Fab')2 fraction and in the low molecular weight peptides derived from the Fc domains. Alpha-1-acid glycoprotein, ribonuclease, and lysozyme are also labelled by this procedure. Enhancement of 75Se incorporation by urea, guanidinium chloride, mercaptoethanol, sodium sulfite and carrier selenite is interpreted as an effect of destabilization of IgG disulfide bonds. Up to 1.4 g atoms Se per mol IgG have been incorporated. We assume that selenite is cleaving disulfides by a process akin to sulfitolysis. The lability of the isolated 75Se-labelled IgG to high concentrations of mercaptans and sulfite is consistent with this idea. These 75Se-labelled proteins may be useful in structure studies and radioimmunoassay.
|
Reaction of selenium with immunoglobulin molecules. Radioactive selenite reacts with purified human and goat immunoglobulins at acidic and neutral pH. The antigenic properties of the immunoglobulins are retained during the selenium labelling as shown by immunoelectrophoresis and autoradiography. Pepsin digests of 75Se-labelled IgG possess 75Se both in the (Fab')2 fraction and in the low molecular weight peptides derived from the Fc domains. Alpha-1-acid glycoprotein, ribonuclease, and lysozyme are also labelled by this procedure. Enhancement of 75Se incorporation by urea, guanidinium chloride, mercaptoethanol, sodium sulfite and carrier selenite is interpreted as an effect of destabilization of IgG disulfide bonds. Up to 1.4 g atoms Se per mol IgG have been incorporated. We assume that selenite is cleaving disulfides by a process akin to sulfitolysis. The lability of the isolated 75Se-labelled IgG to high concentrations of mercaptans and sulfite is consistent with this idea. These 75Se-labelled proteins may be useful in structure studies and radioimmunoassay.
|
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-0.08116684854030609,
0.003124149516224861,
-0.026928192004561424,
-0.035339854657649994,
-0.022249039262533188,
0.014106138609349728,
-0.008480365388095379,
0.0011450705351307988,
-0.017316605895757675,
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0.09164197742938995,
0.013490241952240467
] |
PMID:19085
|
Magnetic circular dichroism studies on acid and alkaline forms of horseradish peroxidase.
|
The heme vicinities of the acid and alkaline forms of native (Fd(III)) horseradish peroxidase were investigated in terms of the magnetic circular dichroism (MCD) spectroscopy. The MCD spectrum of the acid form of native horseradish peroxidase was characteristic of a ferric high spin heme group. The resemblance in the MCD spectrum between the acid form and acetato-iron (III)protoporphyrin IX dimethyl ester suggests that the heme iron of the acid form has the electronic structure similar to that in a pentocoordinated heme complex. The MCD spectra of native horseradish peroxidase did not shown any substantial pH dependence in the pH range from 5.20 to 9.00. The MCD spectral change indicated the pK value for the equilibrium between the acid and alkaline forms to be 11.0 which agrees with the results from other methods. The alkaline form of native horseradish peroxidase at pH 12.01 exhibited the MCD spectrum of a low spin complex. The near infrared MCD spectrum suggests that the alkaline form of native horseradish peroxidase has a 6th ligand somehow different from a normal nitrogen ligand such as histidine or lysine. It implicates that the alkaline form has an overall ligand field strength of between the low spin component of metmyoglobin hydroxide and metmyoglobin azide.
|
Magnetic circular dichroism studies on acid and alkaline forms of horseradish peroxidase. The heme vicinities of the acid and alkaline forms of native (Fd(III)) horseradish peroxidase were investigated in terms of the magnetic circular dichroism (MCD) spectroscopy. The MCD spectrum of the acid form of native horseradish peroxidase was characteristic of a ferric high spin heme group. The resemblance in the MCD spectrum between the acid form and acetato-iron (III)protoporphyrin IX dimethyl ester suggests that the heme iron of the acid form has the electronic structure similar to that in a pentocoordinated heme complex. The MCD spectra of native horseradish peroxidase did not shown any substantial pH dependence in the pH range from 5.20 to 9.00. The MCD spectral change indicated the pK value for the equilibrium between the acid and alkaline forms to be 11.0 which agrees with the results from other methods. The alkaline form of native horseradish peroxidase at pH 12.01 exhibited the MCD spectrum of a low spin complex. The near infrared MCD spectrum suggests that the alkaline form of native horseradish peroxidase has a 6th ligand somehow different from a normal nitrogen ligand such as histidine or lysine. It implicates that the alkaline form has an overall ligand field strength of between the low spin component of metmyoglobin hydroxide and metmyoglobin azide.
|
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] |
PMID:19086
|
Circular dichroism and conformation of human alpha1-antitrypsin.
|
The solution conformation of alpha 1-antitrypsin from human blood plasma was studied by the circular dichroism (CD) probe. The CD spectra revealed in this glycoprotein approximately 16-20% of alpha-helix, the rest of the main polypeptide chain possessing the pleated sheet (beta) and the aperiodic structures. The conformation was stable between pH 4.7 and 8.8. Reversible change in conformation was observed at pH 10.3, and more dratic denaturation occurred at pH 11.6. The environment of the side chain chromophores was strongly affected by acid at pH 2.5, whereas the main chain conformation was changed slightly. A drastic change in the CD spectra, indicating denaturation, was observed in 3.5 M guanidine hydrochloride. Sodium dodecyl sulfate was effective in disorganizing the tertiary structure and in enhancing the helix content. The phenylalanine band fine structure was observed in the native protein and also after denaturation with acid, guanidine hydrochloride and sodium dodecyl sulfate.
|
Circular dichroism and conformation of human alpha1-antitrypsin. The solution conformation of alpha 1-antitrypsin from human blood plasma was studied by the circular dichroism (CD) probe. The CD spectra revealed in this glycoprotein approximately 16-20% of alpha-helix, the rest of the main polypeptide chain possessing the pleated sheet (beta) and the aperiodic structures. The conformation was stable between pH 4.7 and 8.8. Reversible change in conformation was observed at pH 10.3, and more dratic denaturation occurred at pH 11.6. The environment of the side chain chromophores was strongly affected by acid at pH 2.5, whereas the main chain conformation was changed slightly. A drastic change in the CD spectra, indicating denaturation, was observed in 3.5 M guanidine hydrochloride. Sodium dodecyl sulfate was effective in disorganizing the tertiary structure and in enhancing the helix content. The phenylalanine band fine structure was observed in the native protein and also after denaturation with acid, guanidine hydrochloride and sodium dodecyl sulfate.
|
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] |
PMID:19087
|
Iron exchange between transferrin molecules mediated by phosphate compounds and other cell metabolites.
|
The ability of a large number of cellular metabolites to release iron from transferrin was investigated by measuring the rate at which they could mediate iron exchange between two types of transferrin. Rabbit transferrin labelled with 59Fe was incubated with human apotransferrin in the presence of the metabolites. After varying periods of incubation the human transferrin was separated from the rabbit transferrin by immunoprecipitation. GTP, 2,3-diphosphoglycerate, ATP, ADP and citrate produced the most rapid exchange of iron between the two types of transferrin, but many other compounds showed some degree of activity. Iron exchange mediated by the organic phosphates had the characteristics of a single first-order reaction and was sensitive to changes of incubation temperature and pH. The activation energy for the exchange reaction was approx. 13 kcal/mol. The rate of iron exchange from the oxalate - iron - transferrin complex was much lower than from bicarbonate - iron - transferrin. It is concluded that several organic phosphates have the capacity of releasing iron from transferrin. These compounds may represent the means by which the iron is released during the process of cellular uptake.
|
Iron exchange between transferrin molecules mediated by phosphate compounds and other cell metabolites. The ability of a large number of cellular metabolites to release iron from transferrin was investigated by measuring the rate at which they could mediate iron exchange between two types of transferrin. Rabbit transferrin labelled with 59Fe was incubated with human apotransferrin in the presence of the metabolites. After varying periods of incubation the human transferrin was separated from the rabbit transferrin by immunoprecipitation. GTP, 2,3-diphosphoglycerate, ATP, ADP and citrate produced the most rapid exchange of iron between the two types of transferrin, but many other compounds showed some degree of activity. Iron exchange mediated by the organic phosphates had the characteristics of a single first-order reaction and was sensitive to changes of incubation temperature and pH. The activation energy for the exchange reaction was approx. 13 kcal/mol. The rate of iron exchange from the oxalate - iron - transferrin complex was much lower than from bicarbonate - iron - transferrin. It is concluded that several organic phosphates have the capacity of releasing iron from transferrin. These compounds may represent the means by which the iron is released during the process of cellular uptake.
|
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] |
PMID:19088
|
Contribution of pH-sensitive metabolic processes to pH homeostasis in isolated rat kidney tubules.
|
The metabolism of isolated rat kidney tubules suspended in calcium-free physiological saline buffered with phosphate was found to be sensitive to changes in the pH of the suspending medium. Lowering the pH from 7.8 to 6.4 brought about increases in the rates of oxidation of added succinate, glutamate or glutamine as well as in the production of glucose from lactate, glutamine, succinate and fructose. The cellular ATP level was also higher in tubules incubated at pH 6.4 In contrast, the utilization of added glucose was greater at pH 7.8 than at pH 6.4, a substantial amount of lactate being produced at the higher pH. When glucose and either lactate or glutamine were provided as co-substrates glucose was the preferred fuel at pH 7.8 but the alternative substrate was the more readily utilized at pH 6.4. As a consequence of the metabolic activities of the tubules the pH of the suspending medium changed, utilization of lactate, glutamate or glutamine causing a rise in pH while conversion of glucose to lactate caused a fall in pH. In cases where two substrates were metabolized concurrently over a period of 3 h the extracellular pH tended towards a plateau level of approximately pH 7.4. It is proposed that pH-sensitive metabolism in isolated kidney tubules contributes to pH homeostasis in the cellular environment.
|
Contribution of pH-sensitive metabolic processes to pH homeostasis in isolated rat kidney tubules. The metabolism of isolated rat kidney tubules suspended in calcium-free physiological saline buffered with phosphate was found to be sensitive to changes in the pH of the suspending medium. Lowering the pH from 7.8 to 6.4 brought about increases in the rates of oxidation of added succinate, glutamate or glutamine as well as in the production of glucose from lactate, glutamine, succinate and fructose. The cellular ATP level was also higher in tubules incubated at pH 6.4 In contrast, the utilization of added glucose was greater at pH 7.8 than at pH 6.4, a substantial amount of lactate being produced at the higher pH. When glucose and either lactate or glutamine were provided as co-substrates glucose was the preferred fuel at pH 7.8 but the alternative substrate was the more readily utilized at pH 6.4. As a consequence of the metabolic activities of the tubules the pH of the suspending medium changed, utilization of lactate, glutamate or glutamine causing a rise in pH while conversion of glucose to lactate caused a fall in pH. In cases where two substrates were metabolized concurrently over a period of 3 h the extracellular pH tended towards a plateau level of approximately pH 7.4. It is proposed that pH-sensitive metabolism in isolated kidney tubules contributes to pH homeostasis in the cellular environment.
|
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] |
PMID:19091
|
Purification and properties of rat brain succinic semialdehyde dehydrogenase.
|
Succinic semialdehyde dehydrogenase from rat brain has been purified to electrophoretic homogeneity. It has a molecular weight of about 140, 000 and is composed of two apparently identical subunits. The reaction catalized by the pure protein is entirely dependent on endogenous --SH groups. The Kim (limits) for NAD and succinic semialdehyde are 2 X 10(-5) M and 1 X 10(-4) M respectively at the optimum pH of 8.6. Inhibition studies show that the reaction mechanism is a compulsory ordered on where NAD binds first followed by succinic semialdehyde.
|
Purification and properties of rat brain succinic semialdehyde dehydrogenase. Succinic semialdehyde dehydrogenase from rat brain has been purified to electrophoretic homogeneity. It has a molecular weight of about 140, 000 and is composed of two apparently identical subunits. The reaction catalized by the pure protein is entirely dependent on endogenous --SH groups. The Kim (limits) for NAD and succinic semialdehyde are 2 X 10(-5) M and 1 X 10(-4) M respectively at the optimum pH of 8.6. Inhibition studies show that the reaction mechanism is a compulsory ordered on where NAD binds first followed by succinic semialdehyde.
|
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] |
PMID:19089
|
[Role of phycobilin pigments in photosynthesis].
|
Experimental data on possible role of phicobilliprotein (PhBP) in photosynthesis are analysed. It is concluded that the widely spread notion about PhBP only as the light-gathering pigments which transfer the energy to chlorophyll, turned to be insufficiently substantiated experimentally until recently. At the same time the discovered ability of PhBP for reversible redox transformations together with the new data on the nature of fluorescence of blue-green algae and PhBP localization in the cell allowed a suggestion that PhBP can independently of chlorophyll or together with it directly participate in photochemical reactions of photosynthesis. A suggestion is advanced concerning possible existence of the reaction centres of PhBP in phicobillisomes.
|
[Role of phycobilin pigments in photosynthesis]. Experimental data on possible role of phicobilliprotein (PhBP) in photosynthesis are analysed. It is concluded that the widely spread notion about PhBP only as the light-gathering pigments which transfer the energy to chlorophyll, turned to be insufficiently substantiated experimentally until recently. At the same time the discovered ability of PhBP for reversible redox transformations together with the new data on the nature of fluorescence of blue-green algae and PhBP localization in the cell allowed a suggestion that PhBP can independently of chlorophyll or together with it directly participate in photochemical reactions of photosynthesis. A suggestion is advanced concerning possible existence of the reaction centres of PhBP in phicobillisomes.
|
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0.056044451892375946,
0.07285478711128235
] |
PMID:19092
|
Presence of a third sucrose hydrolyzing enzyme in Bacillus subtilis: constitutive levanase synthesis by mutants of Bacillus subtilis Marburg 168.
|
A beta-D-fructofuranosidase -- called levanase -- capable of the hydrolysis of sucrose, inulin and levans has been identified in Bacillus subtilis Marburg. This enzyme can not be detected in strain 168. However, sacL mutations -- mapped on the chromosome of strain 168 between the pheA and aroD reference markers -- lead to constitutive levanase synthesis. This synthesis is repressed by carbon sources such as glucose, glycerol or sucrose.
|
Presence of a third sucrose hydrolyzing enzyme in Bacillus subtilis: constitutive levanase synthesis by mutants of Bacillus subtilis Marburg 168. A beta-D-fructofuranosidase -- called levanase -- capable of the hydrolysis of sucrose, inulin and levans has been identified in Bacillus subtilis Marburg. This enzyme can not be detected in strain 168. However, sacL mutations -- mapped on the chromosome of strain 168 between the pheA and aroD reference markers -- lead to constitutive levanase synthesis. This synthesis is repressed by carbon sources such as glucose, glycerol or sucrose.
|
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] |
PMID:19093
|
[Genetic independence of two forms of carbonic anhydrase from bovine erythrocytes].
|
The two major forms of bovine erythrocyte carbonic anhydrase have been designated as CI and CII because their high activity of the C type. Separation of both forms and isolation of CI from the ethanol chloroform extract of the hemolysate were obtained by either column chromatography on DEAE-cellulose DE 23 or on DEAE-sephadex A-50. But pure preparations of the CII form were only obtained from DEAE-sephadex A-50 which separated CII from a minor component CIv1. Comparative studies of the CI and CII forms and of the minor component CIv1 strongly suggest that CIv1 is a conformational variant of CI and CII are genetic variants differing at least in their primary structure by one Arg yields Gln substitution 56 residues from the N-acetylated terminus. Based on the large variability of the proportion of the two isozymes in heterozygous individuals, the modality of the inheritance of these enzymes is discussed.
|
[Genetic independence of two forms of carbonic anhydrase from bovine erythrocytes]. The two major forms of bovine erythrocyte carbonic anhydrase have been designated as CI and CII because their high activity of the C type. Separation of both forms and isolation of CI from the ethanol chloroform extract of the hemolysate were obtained by either column chromatography on DEAE-cellulose DE 23 or on DEAE-sephadex A-50. But pure preparations of the CII form were only obtained from DEAE-sephadex A-50 which separated CII from a minor component CIv1. Comparative studies of the CI and CII forms and of the minor component CIv1 strongly suggest that CIv1 is a conformational variant of CI and CII are genetic variants differing at least in their primary structure by one Arg yields Gln substitution 56 residues from the N-acetylated terminus. Based on the large variability of the proportion of the two isozymes in heterozygous individuals, the modality of the inheritance of these enzymes is discussed.
|
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] |
PMID:19095
|
A fine-structural study of embryonic and larval development in the gymnoblastic hydroid Pennaria tiarella.
|
1. The pregastrulation blastomers contain electron-dense granules which become localized after gastrulation in the apices of the developing epithelio-muscle cells and persist throughout larval development. The cytoplasm of the blastomeres is organized into anucleate, membrane-delimited lobules. The lobules, which persist until six hours of development, come to contain a single, peripherally located cisterna of granular endoplasmic reticulum. Microvilli are present at the earliest stages examined and persist throughout development. Cilia are first detected at four hours. 2. Gastrulation, marked by the appearance of the mesoglea, occurs between six and eight hours of development. Basal foot processes of epithelio-muscle cells are detected by eight hours, but myonemes cannot be detected until later in development. 3. Immediately following gastrulation, mucous cells begin their differentiation from dividing cells located near the apex of the ectoderm. During their differentiation, the cells elongate toward the mesoglea. 4. By 16 hours post-fertilization, a third cell type can be detected in the ectoderm. The cell, which contains no granules, has an unusual cytoplasmic organization in which fused membranes divide the cytoplasm into parallel compartments containing a single cisterna of granular endoplasmic reticulum. 5. The findings of the present study are correlated with those of previous studies of development in Pennaria and other hydroids. The possible functional roles of the Type I granules, the cytoplasmic lobules, and the nongranular cell are discussed.
|
A fine-structural study of embryonic and larval development in the gymnoblastic hydroid Pennaria tiarella. 1. The pregastrulation blastomers contain electron-dense granules which become localized after gastrulation in the apices of the developing epithelio-muscle cells and persist throughout larval development. The cytoplasm of the blastomeres is organized into anucleate, membrane-delimited lobules. The lobules, which persist until six hours of development, come to contain a single, peripherally located cisterna of granular endoplasmic reticulum. Microvilli are present at the earliest stages examined and persist throughout development. Cilia are first detected at four hours. 2. Gastrulation, marked by the appearance of the mesoglea, occurs between six and eight hours of development. Basal foot processes of epithelio-muscle cells are detected by eight hours, but myonemes cannot be detected until later in development. 3. Immediately following gastrulation, mucous cells begin their differentiation from dividing cells located near the apex of the ectoderm. During their differentiation, the cells elongate toward the mesoglea. 4. By 16 hours post-fertilization, a third cell type can be detected in the ectoderm. The cell, which contains no granules, has an unusual cytoplasmic organization in which fused membranes divide the cytoplasm into parallel compartments containing a single cisterna of granular endoplasmic reticulum. 5. The findings of the present study are correlated with those of previous studies of development in Pennaria and other hydroids. The possible functional roles of the Type I granules, the cytoplasmic lobules, and the nongranular cell are discussed.
|
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0.05014297738671303,
-0.05814399942755699,
0.01218572910875082,
0.06339581310749054,
0.05264617130160332
] |
PMID:19096
|
[Identification and properties of 2 forms of plant phospholipase D].
|
Effect of different factors (pH, temperature etc.) on the activity of phospholipase D is studied. It is found that plant phospholipase D has two forms: thermolabile (D1) and thermostable (Ds). Both forms are shown to differ in some characteristics (pH optimum, temperature optimum, calcium ions activation, activator effect, kinetic parameters, thermostavility). The contradictive literature data on phospholipase D properties are suggested to be due to the existence of two enzyme forms.
|
[Identification and properties of 2 forms of plant phospholipase D]. Effect of different factors (pH, temperature etc.) on the activity of phospholipase D is studied. It is found that plant phospholipase D has two forms: thermolabile (D1) and thermostable (Ds). Both forms are shown to differ in some characteristics (pH optimum, temperature optimum, calcium ions activation, activator effect, kinetic parameters, thermostavility). The contradictive literature data on phospholipase D properties are suggested to be due to the existence of two enzyme forms.
|
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] |
PMID:19097
|
[Isolation and properties of leucine aminopeptidase from Aspergillus oryzae].
|
Homogenious leucine aminopeptidase is purified from "oryzine"--mixture of enzymes produced by surface culture of Asperigillus oryzae using treatment with activated characoal, followed by DEAE-cellulose and hydroxylapatite chromatographies, Biogel P-100 gel-filtration and polyacrylamide-gel electrophoresis. The enzyme has pH optimum 9.0 and the molecular weight 37500 as estimated by gil-filtration through Sephadex G-100 (superfine) and SDS-polyacrylamide gel electrophoresis. Leucine aminopeptidase from Asp. oryzae has a broad substrate specificity, therefore, cleaving with the highest rate the peptides carrying N-terminal leucine. The enzyme is completely inhibited with EDTA and beta-mercaptoethanol, and it is a metalloenzyme.
|
[Isolation and properties of leucine aminopeptidase from Aspergillus oryzae]. Homogenious leucine aminopeptidase is purified from "oryzine"--mixture of enzymes produced by surface culture of Asperigillus oryzae using treatment with activated characoal, followed by DEAE-cellulose and hydroxylapatite chromatographies, Biogel P-100 gel-filtration and polyacrylamide-gel electrophoresis. The enzyme has pH optimum 9.0 and the molecular weight 37500 as estimated by gil-filtration through Sephadex G-100 (superfine) and SDS-polyacrylamide gel electrophoresis. Leucine aminopeptidase from Asp. oryzae has a broad substrate specificity, therefore, cleaving with the highest rate the peptides carrying N-terminal leucine. The enzyme is completely inhibited with EDTA and beta-mercaptoethanol, and it is a metalloenzyme.
|
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] |
PMID:19098
|
[Malic acid induction of decarboxylating NADP-malate dehydrogenase synthesis in C3-plant leaves].
|
The activity of decarboxylating NADP-malatedehydrogenase (E. C. 1.1.1.40) in green ethiolated pea and barley leaves and in green leaves of a pea mutant lacking photosystem II is found to be 3-fold increased after the injection of malic acid into cut plants. Protein synthesis inhibitors depressed malic acid-induced increase of the activity of "malic"-enzyme, the effect of chloramphenicol being more pronounced in ethiolated green leaves, and that of cycloheximide--in leaves of a mutant with formed photosynthetic apparatus. Possible dependence of malate-induced biosynthesis of "malic"-enzyme on the degree of NADP reduction in chloroplasts is discussed.
|
[Malic acid induction of decarboxylating NADP-malate dehydrogenase synthesis in C3-plant leaves]. The activity of decarboxylating NADP-malatedehydrogenase (E. C. 1.1.1.40) in green ethiolated pea and barley leaves and in green leaves of a pea mutant lacking photosystem II is found to be 3-fold increased after the injection of malic acid into cut plants. Protein synthesis inhibitors depressed malic acid-induced increase of the activity of "malic"-enzyme, the effect of chloramphenicol being more pronounced in ethiolated green leaves, and that of cycloheximide--in leaves of a mutant with formed photosynthetic apparatus. Possible dependence of malate-induced biosynthesis of "malic"-enzyme on the degree of NADP reduction in chloroplasts is discussed.
|
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] |
PMID:19099
|
[Characteristics of acid ribonuclease from rat thymus chromatin].
|
Acid ribonuclease, free of nucleases and phosphatases, is isolated from rat thymus chromatin. The pH optimum of the enzyme is 5.0-5.5, optimal concentrations of Na+ and K+ ions are 0.05-0.15 M and 0.05 M respectively, Mg2+ inhibits the enzyme activity. The enzyme hydrolyses poly U, poly AU, cytoplasmic and nuclear RNAs, but does not attack poly A, polyG, polyC, poly A:poly U, native and denatured DNA'S. The enzyme is 3'-endonuclease, it splits the bond between the 5'-carbon atom of adenosine, guanosine and uridine and 3'-phosphate of uridilic residue. Middle length of oligonucleotides after the hydrolysis of cytoplasmic RNA comprises 10 nucleotides. Possible role of the enzyme in the processing of nuclear RNAs is discussed.
|
[Characteristics of acid ribonuclease from rat thymus chromatin]. Acid ribonuclease, free of nucleases and phosphatases, is isolated from rat thymus chromatin. The pH optimum of the enzyme is 5.0-5.5, optimal concentrations of Na+ and K+ ions are 0.05-0.15 M and 0.05 M respectively, Mg2+ inhibits the enzyme activity. The enzyme hydrolyses poly U, poly AU, cytoplasmic and nuclear RNAs, but does not attack poly A, polyG, polyC, poly A:poly U, native and denatured DNA'S. The enzyme is 3'-endonuclease, it splits the bond between the 5'-carbon atom of adenosine, guanosine and uridine and 3'-phosphate of uridilic residue. Middle length of oligonucleotides after the hydrolysis of cytoplasmic RNA comprises 10 nucleotides. Possible role of the enzyme in the processing of nuclear RNAs is discussed.
|
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] |
PMID:19100
|
[Purification of phospholipase C from Bacillus cereus by chromatography on aminoalkylpolysaccharide adsorbents].
|
Purification of phospholipase C from Bac. cereus by chromatography on aminoalkylpolysaccharide adsorbents is described. The dependence of the degree of enzyme purification on the amount of ligant and effect of pH and buffer systems on the adsorption-desorption of phospholipase have been studied. At a pH below 9.0 phospholipase C is not retained by the adsorbents and is purified 4-5-fold and up to 23-fold, when aminoalkyl-Sepharose and hexamethylenediamine Sephadex are used respectively. With an increase in the pH value up to 10.0, the enzyme is bound by the adsorbent and is eluted with a 40-90% yield of activity and 7-10-fold purification. The resulting phospholipase C is highly purified and electrophoretically homogeneous. A mechanism of the enzyme-adsorbent interaction is discussed.
|
[Purification of phospholipase C from Bacillus cereus by chromatography on aminoalkylpolysaccharide adsorbents]. Purification of phospholipase C from Bac. cereus by chromatography on aminoalkylpolysaccharide adsorbents is described. The dependence of the degree of enzyme purification on the amount of ligant and effect of pH and buffer systems on the adsorption-desorption of phospholipase have been studied. At a pH below 9.0 phospholipase C is not retained by the adsorbents and is purified 4-5-fold and up to 23-fold, when aminoalkyl-Sepharose and hexamethylenediamine Sephadex are used respectively. With an increase in the pH value up to 10.0, the enzyme is bound by the adsorbent and is eluted with a 40-90% yield of activity and 7-10-fold purification. The resulting phospholipase C is highly purified and electrophoretically homogeneous. A mechanism of the enzyme-adsorbent interaction is discussed.
|
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] |
PMID:19101
|
[pH-dependence characteristics of Ca-ATPase activity of heavy meromyosin with modified SH-groups].
|
Study of pH-dependence of Ca-ATPase activity of heavy meromyosin (HMM) at low and high ionic strength showed essential differences in the modifying effect of two sulfhydryl reagents, p-CMB and silver. Silver ions in conditions studied independently on pH and KCl concentration produce an inhibition of ATP hydrolysis by myosin and HMM, the shape of the pH-dependence curve remaining similar to that of the native enzyme up to 40% of blocking free sulfhydryl groups. At the same degree of binding of sulfhydryl groups with p-CMB at 0,5 M KCl the pH-dependence curve due to activation at neutral pH changes it's shape and becomes similar to that for dissociation of two ionizable groups (at neutral and alkaline regions). In contrast to this, a low or zero concentrations of KCl no activation was observed for the enzyme with 40-50% of SH-Groups modified by p-CMB and Ca-ATPase in this case seemed to be independent of pH. The data obtained suggest that SH-Groups are not included into the active site of myosin, and the activating effect observed for some sulfhydryl reagents, is due to conformational changes and it can be the result of the penetrance of the organic part of the reagent molecule into hydrophobic region of the protein.
|
[pH-dependence characteristics of Ca-ATPase activity of heavy meromyosin with modified SH-groups]. Study of pH-dependence of Ca-ATPase activity of heavy meromyosin (HMM) at low and high ionic strength showed essential differences in the modifying effect of two sulfhydryl reagents, p-CMB and silver. Silver ions in conditions studied independently on pH and KCl concentration produce an inhibition of ATP hydrolysis by myosin and HMM, the shape of the pH-dependence curve remaining similar to that of the native enzyme up to 40% of blocking free sulfhydryl groups. At the same degree of binding of sulfhydryl groups with p-CMB at 0,5 M KCl the pH-dependence curve due to activation at neutral pH changes it's shape and becomes similar to that for dissociation of two ionizable groups (at neutral and alkaline regions). In contrast to this, a low or zero concentrations of KCl no activation was observed for the enzyme with 40-50% of SH-Groups modified by p-CMB and Ca-ATPase in this case seemed to be independent of pH. The data obtained suggest that SH-Groups are not included into the active site of myosin, and the activating effect observed for some sulfhydryl reagents, is due to conformational changes and it can be the result of the penetrance of the organic part of the reagent molecule into hydrophobic region of the protein.
|
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] |
PMID:19102
|
[Regulation of glutamine metabolism in Chlorella pyrenoidosa. Regulation of glutamine synthetase activity by adenylic system components].
|
A decrease of glutamine synthetase (E. C. 6.3.1.2.) activity was observed under the assimilation of ammonium nitrogen in Chlorella. At the same time a decrease of ATP content in Chlorella cells took place. The ATP content was 7-fold decreased, while ADP and AMP contents were 4-fold and 3-fold increased respectively, after 15 min. of Chlorella incubation on "ammonium" medium. Further incubation for 45 min, resulted in gradual increase of ATP content and in decrease of ADP and AMP contents. The value of energy charge in ammonium assimilating Chlorella cells sharply decreased for first 15 min. of incubation and then it normalized gradually. The experiments with glutamine synthetase preparation, isolated from ammonium assimilating cells, have shown that ADP and AMP are strong inhibitors of the enzyme in the presence of Mg2+, and only ADP produces the inhibitory effect in the presence of Mn2+. No enzyme reactivation was observed after the transfer of ammonium assimilating cells into nitrogen-free medium or nitrate medium, the enzyme activity increasing at the expense of enzyme protein synthesis denovo.
|
[Regulation of glutamine metabolism in Chlorella pyrenoidosa. Regulation of glutamine synthetase activity by adenylic system components]. A decrease of glutamine synthetase (E. C. 6.3.1.2.) activity was observed under the assimilation of ammonium nitrogen in Chlorella. At the same time a decrease of ATP content in Chlorella cells took place. The ATP content was 7-fold decreased, while ADP and AMP contents were 4-fold and 3-fold increased respectively, after 15 min. of Chlorella incubation on "ammonium" medium. Further incubation for 45 min, resulted in gradual increase of ATP content and in decrease of ADP and AMP contents. The value of energy charge in ammonium assimilating Chlorella cells sharply decreased for first 15 min. of incubation and then it normalized gradually. The experiments with glutamine synthetase preparation, isolated from ammonium assimilating cells, have shown that ADP and AMP are strong inhibitors of the enzyme in the presence of Mg2+, and only ADP produces the inhibitory effect in the presence of Mn2+. No enzyme reactivation was observed after the transfer of ammonium assimilating cells into nitrogen-free medium or nitrate medium, the enzyme activity increasing at the expense of enzyme protein synthesis denovo.
|
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] |
PMID:19103
|
[Oxidation of putrescine, spermidine and spermine by diamino-oxidase from mouse liver].
|
Optimal conditions to determine the activity of diaminooxidase in mouse liver homogenate are described. Maximal oxidation rate for putrescine was found to take place at a concentration of 20 mM and pH 9.5, and for spermidine and spermine--at 10 mM concentration and pH 9.2. The rate of tyramine oxidation was maximal at pH 7.8. Apparent KM values were 4.98-10(-3 M, 1-10(-3) M and 0.8-10(-3) M for putrescine, spermidine and spermine respectively. Hydroxylamine did not inhibit the rate of putrescin oxidation at optimal pH value.
|
[Oxidation of putrescine, spermidine and spermine by diamino-oxidase from mouse liver]. Optimal conditions to determine the activity of diaminooxidase in mouse liver homogenate are described. Maximal oxidation rate for putrescine was found to take place at a concentration of 20 mM and pH 9.5, and for spermidine and spermine--at 10 mM concentration and pH 9.2. The rate of tyramine oxidation was maximal at pH 7.8. Apparent KM values were 4.98-10(-3 M, 1-10(-3) M and 0.8-10(-3) M for putrescine, spermidine and spermine respectively. Hydroxylamine did not inhibit the rate of putrescin oxidation at optimal pH value.
|
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] |
PMID:19104
|
[Fluorescent properties of b-type ferredoxins].
|
Fluroescent spectra of six b-type ferredoxins of plant and animal origins were obtained. All investigated proteins do not contain tryptophan. The emission maxima of the native proteins, apoproteins prepared by various methods, and denaturated proteins are compared. The effects of pH, ionic strength and ferricyanide on the ferredoxins fluorescence were studied. "Unusual" emission at 340nm noted previously for adrenal ferredoxin was observed for spinach and Chenopodium album ferredoxins too. The localization of tyrosine fluorescent maximum at 340nm in the ferredoxins is not due to interaction of tyrosine with the iron-sulfur center. The data obtained allow to suggest that the tyrosine residues in ferredoxins have different environments.
|
[Fluorescent properties of b-type ferredoxins]. Fluroescent spectra of six b-type ferredoxins of plant and animal origins were obtained. All investigated proteins do not contain tryptophan. The emission maxima of the native proteins, apoproteins prepared by various methods, and denaturated proteins are compared. The effects of pH, ionic strength and ferricyanide on the ferredoxins fluorescence were studied. "Unusual" emission at 340nm noted previously for adrenal ferredoxin was observed for spinach and Chenopodium album ferredoxins too. The localization of tyrosine fluorescent maximum at 340nm in the ferredoxins is not due to interaction of tyrosine with the iron-sulfur center. The data obtained allow to suggest that the tyrosine residues in ferredoxins have different environments.
|
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] |
PMID:19105
|
[Relationships of photoreduction of substituted salts of 4,4'-dipyridyl by isolated chloroplasts].
|
Kinetic relationships of photoreduction of 4,4'-dimethyldipyridyl and 4,4'-dibenzyldipyridyl in the presence of chlorplast were studied. It was found that photoreduction leads to the establishment of photosteady state in which the rate of photoreduction is equal to the rate of dark oxidation of reduced form. Kinetics of dark oxidation of photoreduced form were investigated. The study of inhibition of photoreduction of methylviologen and potassium ferricyanide by diuron was performed. It was shown that the nature of inhibition of both reactions is completely identical. The effect of hydrogen ions concentration and gas phase composition was studied. Stabilization of low potential electron acceptors to the oxidation by molecular oxygen in the reaction of photooxidation of water is discussed.
|
[Relationships of photoreduction of substituted salts of 4,4'-dipyridyl by isolated chloroplasts]. Kinetic relationships of photoreduction of 4,4'-dimethyldipyridyl and 4,4'-dibenzyldipyridyl in the presence of chlorplast were studied. It was found that photoreduction leads to the establishment of photosteady state in which the rate of photoreduction is equal to the rate of dark oxidation of reduced form. Kinetics of dark oxidation of photoreduced form were investigated. The study of inhibition of photoreduction of methylviologen and potassium ferricyanide by diuron was performed. It was shown that the nature of inhibition of both reactions is completely identical. The effect of hydrogen ions concentration and gas phase composition was studied. Stabilization of low potential electron acceptors to the oxidation by molecular oxygen in the reaction of photooxidation of water is discussed.
|
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] |
PMID:19106
|
[Some pathways of biosynthesis and degradation of polyphosphates from green algae Acetabularia mediterranea].
|
The activity of ATP: polyphosphate phosphotransferase was detected in free-cellular extracts of Acetabularia mediterranea. The enzyme activity in cells originally deficient in phosphorus and subsequently transferred into the phosphate-containing medium increases 5-10-fold as compared to normal. Polyphosphate degradation in A. mediterranea is probably produced by polyphosphatase, which was also detected in the free-cellular extract. It was shown that the polyphosphatase activity has two pH optima, i.e. 4.5 and 7.5, and is considerably increased when the cells are transferred into the phosphate-free medium. It is assumed that high-molecular polyphosphates involved in A. Mediterranea metabolism are responsible for regulation of orthophosphate and ATP level in the cells by ATP: polyphosphate phosphotransferase and polyphosphatase.
|
[Some pathways of biosynthesis and degradation of polyphosphates from green algae Acetabularia mediterranea]. The activity of ATP: polyphosphate phosphotransferase was detected in free-cellular extracts of Acetabularia mediterranea. The enzyme activity in cells originally deficient in phosphorus and subsequently transferred into the phosphate-containing medium increases 5-10-fold as compared to normal. Polyphosphate degradation in A. mediterranea is probably produced by polyphosphatase, which was also detected in the free-cellular extract. It was shown that the polyphosphatase activity has two pH optima, i.e. 4.5 and 7.5, and is considerably increased when the cells are transferred into the phosphate-free medium. It is assumed that high-molecular polyphosphates involved in A. Mediterranea metabolism are responsible for regulation of orthophosphate and ATP level in the cells by ATP: polyphosphate phosphotransferase and polyphosphatase.
|
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] |
PMID:19107
|
[Photophosphorylation, sensitized by chlorophills a and b, pheophytin and beta-carotene in a modelled system].
|
In aqueous solutions in air atmosphere chlorophylls a and b, pheophytin and beta-carotene adsorbed on aluminium oxide powder are capable of sensibilizing electron transfer from phosphate ions coupled with the formation of high energy bonds of adenosine phosphates. The highest activity of chlorophylls a and b and pheophytin is observed within the pH range of 7.5-7.8; that of beta-carotene--at pH 7.3-7.5.
|
[Photophosphorylation, sensitized by chlorophills a and b, pheophytin and beta-carotene in a modelled system]. In aqueous solutions in air atmosphere chlorophylls a and b, pheophytin and beta-carotene adsorbed on aluminium oxide powder are capable of sensibilizing electron transfer from phosphate ions coupled with the formation of high energy bonds of adenosine phosphates. The highest activity of chlorophylls a and b and pheophytin is observed within the pH range of 7.5-7.8; that of beta-carotene--at pH 7.3-7.5.
|
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] |
PMID:19109
|
Structure and fragmentation mechanisms of some ions in the mass spectrum of ephedrine.
|
This paper describes the use of gas chromatography mass spectrometry for the confirmation of ephedrine in adulterated powdered ipecac and ipecac fluid extract. Deuteration studies of ephedrine hydrochloride and some related compounds were also performed in an attempt to postulate structures for some of the fragment ions appearing in the spectrum of ephedrine.
|
Structure and fragmentation mechanisms of some ions in the mass spectrum of ephedrine. This paper describes the use of gas chromatography mass spectrometry for the confirmation of ephedrine in adulterated powdered ipecac and ipecac fluid extract. Deuteration studies of ephedrine hydrochloride and some related compounds were also performed in an attempt to postulate structures for some of the fragment ions appearing in the spectrum of ephedrine.
|
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] |
PMID:19110
|
Process engineering studies on immobilized trypsin using molecular sieves as carriers.
|
In the present investigation molecular sieve has been found to be a suitable carrier for the immobilization of enzymes. From the present study it may be specifically found that trypsin and pappain can be immobilized by molecular sieve type 4a following a very simple techniqure. The immobilized enzyme can be used both in packed as well as in a continuous stirred tank reactor (CSTR).
|
Process engineering studies on immobilized trypsin using molecular sieves as carriers. In the present investigation molecular sieve has been found to be a suitable carrier for the immobilization of enzymes. From the present study it may be specifically found that trypsin and pappain can be immobilized by molecular sieve type 4a following a very simple techniqure. The immobilized enzyme can be used both in packed as well as in a continuous stirred tank reactor (CSTR).
|
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] |
PMID:19111
|
Properties and biodegradation of a bioemulsifier from Corynebacterium hydrocarboclastus.
|
An extracellular polymer was produced by continuous fermentation of Corynebacterium hydrocarboclastus on kerosene in a 24 liter reactor. This polymer was composed of protein, lipid, and carbohydrates. The polymer possessed surface active properties, and had two critical micelle concentrations. Its effectiveness was quite comparable to the effectiveness of synthetic surface active agents such as Tween 80 and Span 20; however, its efficiency was much lower. The polymer also had emulsifying properties. Maximum emulsification was obtained at pH 6. The emulsifying properties were unaffected by high salt concentration [up to 5% (w/v) in Na+], and tolerated a water hardness up to 5,000 ppm. A 2 hr treatment of the polymer at temperatures higher than 65 degrees C resulted in a loss of its emulsifying properties. Two microorganisms, named SLYS and Y, isolated from soil, were able to grow on the polymer as sole carbon and energy source, thus proving its biodegradability. SLYS was tentatively identified as Flavobacterium breve and Y as Flavobacterium devorans.
|
Properties and biodegradation of a bioemulsifier from Corynebacterium hydrocarboclastus. An extracellular polymer was produced by continuous fermentation of Corynebacterium hydrocarboclastus on kerosene in a 24 liter reactor. This polymer was composed of protein, lipid, and carbohydrates. The polymer possessed surface active properties, and had two critical micelle concentrations. Its effectiveness was quite comparable to the effectiveness of synthetic surface active agents such as Tween 80 and Span 20; however, its efficiency was much lower. The polymer also had emulsifying properties. Maximum emulsification was obtained at pH 6. The emulsifying properties were unaffected by high salt concentration [up to 5% (w/v) in Na+], and tolerated a water hardness up to 5,000 ppm. A 2 hr treatment of the polymer at temperatures higher than 65 degrees C resulted in a loss of its emulsifying properties. Two microorganisms, named SLYS and Y, isolated from soil, were able to grow on the polymer as sole carbon and energy source, thus proving its biodegradability. SLYS was tentatively identified as Flavobacterium breve and Y as Flavobacterium devorans.
|
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] |
PMID:19112
|
1,4-alpha-Glucan phosphorylase form Klebsiella pneumoniae covalently couple on porous glass.
|
A simplified procedure for the preparation of 1,4-alpha-glucan phosphorylase from Klebsiella pneumoniae is described. An 80-fold purification is achieved in two steps with an overall yield of about 50%. The specific activity of the homogeneous enzyme protein is 17.7 units/mg. Compared with glycogen phosphorylase from rabbit muscle the enzyme from K. pneumoniae shows a markedly higher stability against deforming and chaotropic agents. The 1,4-alpha-glucan phosphorylase was covalently bound to porous glass particles by three different methods. Coupling with glutaraldehyde gave the highest specific activity, i.e., 5.6 units/mg of bound protein or 133 units/g of glass with maltodextrin as substrate. This corresponds to about 30% of the specific activity of the soluble enzyme. With substrates of higher molecular weight, such as glycogen or amylopectin, lower relative activity was observed. The immobilized enzyme preparations showed pH activity profiles which were slightly displaced to higher values and exhibited an increased temperature stability.
|
1,4-alpha-Glucan phosphorylase form Klebsiella pneumoniae covalently couple on porous glass. A simplified procedure for the preparation of 1,4-alpha-glucan phosphorylase from Klebsiella pneumoniae is described. An 80-fold purification is achieved in two steps with an overall yield of about 50%. The specific activity of the homogeneous enzyme protein is 17.7 units/mg. Compared with glycogen phosphorylase from rabbit muscle the enzyme from K. pneumoniae shows a markedly higher stability against deforming and chaotropic agents. The 1,4-alpha-glucan phosphorylase was covalently bound to porous glass particles by three different methods. Coupling with glutaraldehyde gave the highest specific activity, i.e., 5.6 units/mg of bound protein or 133 units/g of glass with maltodextrin as substrate. This corresponds to about 30% of the specific activity of the soluble enzyme. With substrates of higher molecular weight, such as glycogen or amylopectin, lower relative activity was observed. The immobilized enzyme preparations showed pH activity profiles which were slightly displaced to higher values and exhibited an increased temperature stability.
|
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] |
PMID:19114
|
Prophylactiv use of propranolol in the Marfan syndrome to prevent aortic dissection.
|
Twenty-five patients, 16 men and 9 women, 5-59 years of age with the Marfan syndrome and cardiac complications were started on propranolol over a 6-year period. Propranolol was used as a beta-adrenergic blocking agent to reduce myocardial contractility in an attempt thereby to stay the progression of aortic dilatation and to prevent acute dissection of the aorta. The indications for prophylactic treatment were aortic dilatation, with aortic regurgitation in most cases. It was intended to keep the pulse rate below 70 at all times or below 60 at rest. Propranolol given in daily doses of 120-160 mg caused no side effects. The mean observation time for propranolol treatment in the 25 patients was 3.0 +/- 1.8 years ranging from 1-7 years. In spite of treatment, 5 patients (1 female and 4 males) experienced acute aortic dissection of rupture with fatal outcome. This occurred in 2 patients with the asthenic type, in 2 patients with the nonasthenic type, and in 1 patient with the marfanoid hypermobility syndrome. Serial echocardiograms showed that other patients on propranolol developed increasing dilatation of the aortic root. These observations indicate that propranolol does not necessarily protect against aortic dissection nor stop the progression of the aortic dilatation when cystic medial necrosis of the aorta is already present.
|
Prophylactiv use of propranolol in the Marfan syndrome to prevent aortic dissection. Twenty-five patients, 16 men and 9 women, 5-59 years of age with the Marfan syndrome and cardiac complications were started on propranolol over a 6-year period. Propranolol was used as a beta-adrenergic blocking agent to reduce myocardial contractility in an attempt thereby to stay the progression of aortic dilatation and to prevent acute dissection of the aorta. The indications for prophylactic treatment were aortic dilatation, with aortic regurgitation in most cases. It was intended to keep the pulse rate below 70 at all times or below 60 at rest. Propranolol given in daily doses of 120-160 mg caused no side effects. The mean observation time for propranolol treatment in the 25 patients was 3.0 +/- 1.8 years ranging from 1-7 years. In spite of treatment, 5 patients (1 female and 4 males) experienced acute aortic dissection of rupture with fatal outcome. This occurred in 2 patients with the asthenic type, in 2 patients with the nonasthenic type, and in 1 patient with the marfanoid hypermobility syndrome. Serial echocardiograms showed that other patients on propranolol developed increasing dilatation of the aortic root. These observations indicate that propranolol does not necessarily protect against aortic dissection nor stop the progression of the aortic dilatation when cystic medial necrosis of the aorta is already present.
|
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] |
PMID:19115
|
The interaction of some bis-arylhydroxysulphonic acids with a site of known structure in human haemoglobin.
|
1 Two bis-arylhydroxysulphonic acids were previously designed to interact with the known molecular configuration of the 2,3-diphosphoglycerate (DPG) receptor-site of human haemoglobin. These compounds liberate oxygen from the haemoglobin similarly to DPG. 2 Solutions of haemoglobin have now been observed under physiological conditions by nuclear magnetic resonance (n.m.r.) in the presence of DPG and of the compounds. 3 Two peaks in the n.m.r. spectrum of haemoglobin are shifted when DPG is added to the solution. 4 The same two peaks in the spectrum are affected by the compounds. 5 The observations are compatible with the predicted interaction between the compounds and the haemoglobin receptor site.
|
The interaction of some bis-arylhydroxysulphonic acids with a site of known structure in human haemoglobin. 1 Two bis-arylhydroxysulphonic acids were previously designed to interact with the known molecular configuration of the 2,3-diphosphoglycerate (DPG) receptor-site of human haemoglobin. These compounds liberate oxygen from the haemoglobin similarly to DPG. 2 Solutions of haemoglobin have now been observed under physiological conditions by nuclear magnetic resonance (n.m.r.) in the presence of DPG and of the compounds. 3 Two peaks in the n.m.r. spectrum of haemoglobin are shifted when DPG is added to the solution. 4 The same two peaks in the spectrum are affected by the compounds. 5 The observations are compatible with the predicted interaction between the compounds and the haemoglobin receptor site.
|
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] |
PMID:19116
|
A potent new beta2-adrenoceptor blocking agent.
|
1 (t-Butyl-amino-3-ol-2-propyl) oximino-9 fluorene is a new beta2-adrenoceptor blocking agent with a pA2 of 9.23+/-0.25 on isolated trachea. 2 It provokes hypertension in normotensive rats and does not prevent arterial hypertension in SHR rats, although it does prevent the renin secretion normally induced by isoprenaline infusion.
|
A potent new beta2-adrenoceptor blocking agent. 1 (t-Butyl-amino-3-ol-2-propyl) oximino-9 fluorene is a new beta2-adrenoceptor blocking agent with a pA2 of 9.23+/-0.25 on isolated trachea. 2 It provokes hypertension in normotensive rats and does not prevent arterial hypertension in SHR rats, although it does prevent the renin secretion normally induced by isoprenaline infusion.
|
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] |
PMID:19117
|
Some observations on the mechanism of benzodiazepine-barbiturate interactions in the mouse.
|
1 The prolongation of pentobarbitone sleeping by five benzodiazepines, administered by prior intraperitoneal injection, was measured in mice. The pentobarbitone was injected either intraperitoneally or intracerebroventricularly. For each benzodiazepine, the prolongation was dose-related and differences in potency between benzodiazepines were not marked. 2 The percentage prolongation of sleeping times produced by most of the benzodiazepines was greater when the pentobarbitone was given intracerebroventricularly and was explained by a preferential addition of CNS depressant effects associated with this route. 3 To test whether the action of intraperitoneally administered pentobarbitone had been influenced by a metabolic component, the effects of nitrazepam on drug metabolism, measured by changes in plasma phenazone levels in the mouse, were studied. Nitrazepam (32 mg/kg, i.p.) produced a 23% reduction in the rate of phenazone metabolism. 4 Nitrazepam was also shown to have produced a transient fall in body temperature. Calculations based on Q10 values suggested that this hypothermia accounted, at most, for half the metabolic change measured.
|
Some observations on the mechanism of benzodiazepine-barbiturate interactions in the mouse. 1 The prolongation of pentobarbitone sleeping by five benzodiazepines, administered by prior intraperitoneal injection, was measured in mice. The pentobarbitone was injected either intraperitoneally or intracerebroventricularly. For each benzodiazepine, the prolongation was dose-related and differences in potency between benzodiazepines were not marked. 2 The percentage prolongation of sleeping times produced by most of the benzodiazepines was greater when the pentobarbitone was given intracerebroventricularly and was explained by a preferential addition of CNS depressant effects associated with this route. 3 To test whether the action of intraperitoneally administered pentobarbitone had been influenced by a metabolic component, the effects of nitrazepam on drug metabolism, measured by changes in plasma phenazone levels in the mouse, were studied. Nitrazepam (32 mg/kg, i.p.) produced a 23% reduction in the rate of phenazone metabolism. 4 Nitrazepam was also shown to have produced a transient fall in body temperature. Calculations based on Q10 values suggested that this hypothermia accounted, at most, for half the metabolic change measured.
|
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] |
PMID:19118
|
Studies on the cardiovascular effects of pindolol in DOCA/saline hypertensive rats.
|
1 A hypotensive response to orally administered pindolol in conscious normotensive and deoxycorticosterone acetate (DOCA)/saline hypertensive rats (DS-rats) is described. In DS-rats, pindolol (10-50 mug/kg) produced a dose-dependent fall in blood pressure and elevation of resting heart rate.2 The hypotensive response and tachycardia produced by oral pindolol (50 mug/kg) in DS-rats were prevented by propranolol (5 mg/kg), suggesting that pindolol's effects are mediated by beta-adrenoceptor stimulation.3 After mecamylamine (10 mg/kg), oral pindolol (50 mug/kg) produced a further fall in blood pressure in DS-rats, suggesting that its hypotensive effects are probably mediated in the peripheral vasculature.4 Pretreatment with oral pindolol (10 or 50 mug/kg) resulted in a reduction of neuronally-induced tachycardia in pithed DS-rats; neuronally-evoked pressor effects were also antagonized by pindolol (50 mug/kg, orally).5 Whereas pindolol, 50 mug/kg orally or intraperitoneally, produced a marked and progressive hypotensive response of rapid onset (20 min) in DS-rats the same dose intravenously produced a smaller response of delayed onset (80 minutes).6 In anaesthetized DS-rats, an equivalent degree of cardiac beta-adrenoceptor blockade was produced by pretreatment with pindolol, 50 mug/kg orally (2 h previously) or intravenously (1 h previously).7 After administration of pindolol, 2 mg/kg intravenously, to conscious DS-rats, the tachycardia produced by intravenous isoprenaline, 3 mug/kg, was almost abolished for the first 60 min of the study, whereas a hypotensive response to pindolol was delayed in onset (100 minutes).8 The hypotensive response and tachycardia produced by oral pindolol 50 mug/kg, in DS-rats were prevented by inhibition of metabolic enzyme activity by pretreatment with Proadifen (SKF 525-A), 80 mg/kg.9 The results suggest that pindolol's effects on blood pressure and heart rate in the conscious DS-rat are mediated by a metabolite(s) acting by stimulation of peripheral beta-adrenoceptors.
|
Studies on the cardiovascular effects of pindolol in DOCA/saline hypertensive rats. 1 A hypotensive response to orally administered pindolol in conscious normotensive and deoxycorticosterone acetate (DOCA)/saline hypertensive rats (DS-rats) is described. In DS-rats, pindolol (10-50 mug/kg) produced a dose-dependent fall in blood pressure and elevation of resting heart rate.2 The hypotensive response and tachycardia produced by oral pindolol (50 mug/kg) in DS-rats were prevented by propranolol (5 mg/kg), suggesting that pindolol's effects are mediated by beta-adrenoceptor stimulation.3 After mecamylamine (10 mg/kg), oral pindolol (50 mug/kg) produced a further fall in blood pressure in DS-rats, suggesting that its hypotensive effects are probably mediated in the peripheral vasculature.4 Pretreatment with oral pindolol (10 or 50 mug/kg) resulted in a reduction of neuronally-induced tachycardia in pithed DS-rats; neuronally-evoked pressor effects were also antagonized by pindolol (50 mug/kg, orally).5 Whereas pindolol, 50 mug/kg orally or intraperitoneally, produced a marked and progressive hypotensive response of rapid onset (20 min) in DS-rats the same dose intravenously produced a smaller response of delayed onset (80 minutes).6 In anaesthetized DS-rats, an equivalent degree of cardiac beta-adrenoceptor blockade was produced by pretreatment with pindolol, 50 mug/kg orally (2 h previously) or intravenously (1 h previously).7 After administration of pindolol, 2 mg/kg intravenously, to conscious DS-rats, the tachycardia produced by intravenous isoprenaline, 3 mug/kg, was almost abolished for the first 60 min of the study, whereas a hypotensive response to pindolol was delayed in onset (100 minutes).8 The hypotensive response and tachycardia produced by oral pindolol 50 mug/kg, in DS-rats were prevented by inhibition of metabolic enzyme activity by pretreatment with Proadifen (SKF 525-A), 80 mg/kg.9 The results suggest that pindolol's effects on blood pressure and heart rate in the conscious DS-rat are mediated by a metabolite(s) acting by stimulation of peripheral beta-adrenoceptors.
|
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] |
PMID:19119
|
An evaluation of viability tests of human cadaveric kidneys.
|
Cadaveric kidneys are sometimes unsuitable for transplantation because of possible ischaemic damage. The advent of perfusion preservation machines has enabled evaluation of perfusion characteristics and perfusate changes of organs prior to transplantation. This study has evaluated the changes in perfusate pH, lacate dehydrogenase, lactate and free fatty acid utilization in an attempt to identify those kidneys with ischaemic damage. In this investigation no single factor was discriminatory and it was not possible to predict with any degree of certainty those kidneys liable to delayed function or to non-function.
|
An evaluation of viability tests of human cadaveric kidneys. Cadaveric kidneys are sometimes unsuitable for transplantation because of possible ischaemic damage. The advent of perfusion preservation machines has enabled evaluation of perfusion characteristics and perfusate changes of organs prior to transplantation. This study has evaluated the changes in perfusate pH, lacate dehydrogenase, lactate and free fatty acid utilization in an attempt to identify those kidneys with ischaemic damage. In this investigation no single factor was discriminatory and it was not possible to predict with any degree of certainty those kidneys liable to delayed function or to non-function.
|
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] |
PMID:19120
|
Where is your vagotomy incomplete? Observations on operative technique.
|
There is a trend in gastric surgery towards more selective types of vagotomy but the techniques are more difficult and incomplete nerve section may be more likely. Using the Grassi intra-operative test of mucosal pH, we have studied 50 consecutive patients, 13 having truncal vagotomy, 9 having bilateral selective vagotomy and 28 having proximal gastric vagotomy. We have identified four distinct areas of the stomach where nerve fibres are likely to be left. Three of these can usually be eliminated by careful attention to technique, but the fourth--the distal extent of the parietalcell mass--can only be identified by a precise intra-operative test; this is relevant to proximal gastric vagotomy but not to truncal vagotomy. Unexpected anatomical variations of the vagus nerve branches were found in 8 patients. A precise intra-operative test of residual innervation is particularly helpful in establishing the technique of proximal gastric vagotomy.
|
Where is your vagotomy incomplete? Observations on operative technique. There is a trend in gastric surgery towards more selective types of vagotomy but the techniques are more difficult and incomplete nerve section may be more likely. Using the Grassi intra-operative test of mucosal pH, we have studied 50 consecutive patients, 13 having truncal vagotomy, 9 having bilateral selective vagotomy and 28 having proximal gastric vagotomy. We have identified four distinct areas of the stomach where nerve fibres are likely to be left. Three of these can usually be eliminated by careful attention to technique, but the fourth--the distal extent of the parietalcell mass--can only be identified by a precise intra-operative test; this is relevant to proximal gastric vagotomy but not to truncal vagotomy. Unexpected anatomical variations of the vagus nerve branches were found in 8 patients. A precise intra-operative test of residual innervation is particularly helpful in establishing the technique of proximal gastric vagotomy.
|
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] |
PMID:19122
|
Increased exercise tolerance with nitrates in beta-blockaded patients with angina.
|
In 14 beta-blockaded anginal subjects, 10 of whom had poor left ventricular function, sublingual isosorbide dinitrate significantly increased maximal exercise capacity on a standardized multistage treadmill test. This was associated with changes in heart rate and blood pressure suggestive of a fall in left ventricular work. The effect of isosorbide lasts for at least two hours and when taken before exercise may be a useful addition to beta-blockade in patients with angina.
|
Increased exercise tolerance with nitrates in beta-blockaded patients with angina. In 14 beta-blockaded anginal subjects, 10 of whom had poor left ventricular function, sublingual isosorbide dinitrate significantly increased maximal exercise capacity on a standardized multistage treadmill test. This was associated with changes in heart rate and blood pressure suggestive of a fall in left ventricular work. The effect of isosorbide lasts for at least two hours and when taken before exercise may be a useful addition to beta-blockade in patients with angina.
|
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] |
PMID:19125
|
A serotonergic innervation of noradrenergic neurons in nucleus locus coeruleus: demonstration by immunocytochemical localization of the transmitter specific enzymes tyrosine and tryptophan hydroxylase.
|
Immunocytochemical localization of the neurotransmitter synthesizing enzymes, tyrosine and tryptophan hydroxylase, was used to determine whether the noradrenergic neurons in the nucleus locus coeruleus of the rat are innervated by serotonergic (5-HT) neurons. Specific antibodies were prepared to tyrosine hydroxylase, purified from the bovine adrenal medulla, and tryptophan hydroxylase, purified from rat midbrain. These were localized by both light and electron microscopy by the use of the peroxidase-antiperoxidase method. In the nucleus locus coeruleus, tyrosine hydroxylase was contained in the cytoplasm, proximal axons, and dendrites of intrinsic neurons. Tryptophan hydroxylase, on the other hand, was only contained within processes surrounding the perikarya and dendrites of the catecholaminergic neurons. The processes labeled with tryptophan hydroxylase were unmyelinated, ranged in size from 0.1 to 1.4 micron, and consisted of terminal varicosities separated by intervaricose segments. Although in close approximation to noradrenergic neurons, these processes, presumably axons, rarely formed synatic contacts with thickened membrane specializations. In processes, tryptophan hydroxylase was associated with subcellular organelles which had size and distribution of microtubules, and small and large synaptic vesicles. These observations provide a morphological basis to support the hypothesis that the activity of noradrenergic neurons may be modulated by a direct action of 5-HT neurons.
|
A serotonergic innervation of noradrenergic neurons in nucleus locus coeruleus: demonstration by immunocytochemical localization of the transmitter specific enzymes tyrosine and tryptophan hydroxylase. Immunocytochemical localization of the neurotransmitter synthesizing enzymes, tyrosine and tryptophan hydroxylase, was used to determine whether the noradrenergic neurons in the nucleus locus coeruleus of the rat are innervated by serotonergic (5-HT) neurons. Specific antibodies were prepared to tyrosine hydroxylase, purified from the bovine adrenal medulla, and tryptophan hydroxylase, purified from rat midbrain. These were localized by both light and electron microscopy by the use of the peroxidase-antiperoxidase method. In the nucleus locus coeruleus, tyrosine hydroxylase was contained in the cytoplasm, proximal axons, and dendrites of intrinsic neurons. Tryptophan hydroxylase, on the other hand, was only contained within processes surrounding the perikarya and dendrites of the catecholaminergic neurons. The processes labeled with tryptophan hydroxylase were unmyelinated, ranged in size from 0.1 to 1.4 micron, and consisted of terminal varicosities separated by intervaricose segments. Although in close approximation to noradrenergic neurons, these processes, presumably axons, rarely formed synatic contacts with thickened membrane specializations. In processes, tryptophan hydroxylase was associated with subcellular organelles which had size and distribution of microtubules, and small and large synaptic vesicles. These observations provide a morphological basis to support the hypothesis that the activity of noradrenergic neurons may be modulated by a direct action of 5-HT neurons.
|
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] |
PMID:19128
|
Behavioral effects of LSD in the cat: proposal of an animal behavior model for studying the actions of hallucinogenic drugs.
|
In the course of examining the complete dose-response relationship for the behavioral effects of LSD in the cat, we discovered that, in addition to large increases in investigatory and hallucinatory-like responses, two behaviors, not previously reported, are emitted with a high probability under LSD. Beginning from a baseline of essentially zero in saline-treated animals, limb flicks and abortive grooming increase in frequency in direct relation to the dose of LSD administered (2.5, 10, 25 and 50 microgram/kg i.p.) and then decrease at higher doses (100 and 200 microgram/kg). Limb flicks are a species-specific behavior seen in normal cats almost exclusively in response to the presence of a foreign substance, such as water, on the hindpaw or forepaw. In abortive grooming, the cat orients to the body surfaces as if to groom but does not emit the consummatory grooming response (bite, lick or scratch), or emits the response in midair. These behaviors can serve as an animal behavior model for the actions of LSD and related hallucinogens in humans. The specificity of these behavioral changes is indicated by the fact that they are never seen in response to other classes of psychoactive drugs such as D-amphetamine, atropine, caffeine, and cholorpheniramine. They are, however, elicited by compounds such as psilocybin which are structurally and functionally related to LSD. The validity of the model is based on evidence indicating that it is: specific to hallucinogens, dose dependent, observed in a dose range effective in humans, parallels the major parameters of the actions of LSD in humans (see following paper), sensitive, robust, reliable, quantifiable and easy to score.
|
Behavioral effects of LSD in the cat: proposal of an animal behavior model for studying the actions of hallucinogenic drugs. In the course of examining the complete dose-response relationship for the behavioral effects of LSD in the cat, we discovered that, in addition to large increases in investigatory and hallucinatory-like responses, two behaviors, not previously reported, are emitted with a high probability under LSD. Beginning from a baseline of essentially zero in saline-treated animals, limb flicks and abortive grooming increase in frequency in direct relation to the dose of LSD administered (2.5, 10, 25 and 50 microgram/kg i.p.) and then decrease at higher doses (100 and 200 microgram/kg). Limb flicks are a species-specific behavior seen in normal cats almost exclusively in response to the presence of a foreign substance, such as water, on the hindpaw or forepaw. In abortive grooming, the cat orients to the body surfaces as if to groom but does not emit the consummatory grooming response (bite, lick or scratch), or emits the response in midair. These behaviors can serve as an animal behavior model for the actions of LSD and related hallucinogens in humans. The specificity of these behavioral changes is indicated by the fact that they are never seen in response to other classes of psychoactive drugs such as D-amphetamine, atropine, caffeine, and cholorpheniramine. They are, however, elicited by compounds such as psilocybin which are structurally and functionally related to LSD. The validity of the model is based on evidence indicating that it is: specific to hallucinogens, dose dependent, observed in a dose range effective in humans, parallels the major parameters of the actions of LSD in humans (see following paper), sensitive, robust, reliable, quantifiable and easy to score.
|
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] |
PMID:19132
|
[Influence of age and sex on the acute toxicity of two steroid anesthetics in rats].
|
During the newborn period, there is a hight increase of the acute toxicity of two steroid anaesthetics (Hydroxydione, Althesin) given by intraperitoneal route on the rat as also an influence of hormonal conditions.
|
[Influence of age and sex on the acute toxicity of two steroid anesthetics in rats]. During the newborn period, there is a hight increase of the acute toxicity of two steroid anaesthetics (Hydroxydione, Althesin) given by intraperitoneal route on the rat as also an influence of hormonal conditions.
|
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] |
PMID:19133
|
[Lysine decarboxylase in Pseudomonas aeruginosa].
|
The research of lysine, ornithine and arginine decarboxylases has been made for 50 strains of fluorescent Pseudomonas (P. aeruginosa, P. fluorescens, P. putida). By thin layer chromatography, all the strains of Pseudomonas aeruginosa and the fifth of the strains of P. putida had lysine decarboxylase activity at alcaline pH (optimal pH 8) ; Pseudomonas fluorescens did not produce this decarboxylase. Arginine and ornithine decarboxylase are absent for all the strains of fluorescent Pseudomonas.
|
[Lysine decarboxylase in Pseudomonas aeruginosa]. The research of lysine, ornithine and arginine decarboxylases has been made for 50 strains of fluorescent Pseudomonas (P. aeruginosa, P. fluorescens, P. putida). By thin layer chromatography, all the strains of Pseudomonas aeruginosa and the fifth of the strains of P. putida had lysine decarboxylase activity at alcaline pH (optimal pH 8) ; Pseudomonas fluorescens did not produce this decarboxylase. Arginine and ornithine decarboxylase are absent for all the strains of fluorescent Pseudomonas.
|
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] |
PMID:19134
|
Cathepsin D activity in isolated odontoblasts.
|
The presence of an acid proteinase with a high activity has been demonstrated in isolated odontoblast-predentine material from dentinogenically active rat incisors. The enzyme was identified as cathepsin D (EC 3.4.23.5). The possible significance of the enzymatic degradation of proteoglycans and glycosaminoglycans in the course of the calcification process is discussed.
|
Cathepsin D activity in isolated odontoblasts. The presence of an acid proteinase with a high activity has been demonstrated in isolated odontoblast-predentine material from dentinogenically active rat incisors. The enzyme was identified as cathepsin D (EC 3.4.23.5). The possible significance of the enzymatic degradation of proteoglycans and glycosaminoglycans in the course of the calcification process is discussed.
|
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] |
PMID:19135
|
An in vitro and in vivo investigation of mellitate and ethane-1-hydroxy-1,1-diphosphonate in calcium phosphate systems.
|
Comparisons of mellitate (MA) and ethane-1-hydroxy-1,1-diphosphonate (EHDP) have been carried out in studies of enamel etching, calcium phosphate crystal growth and animal calculus deposition. In enamel etch studies at pH 5, 6, or 7 and after treatment times of 5 or 170 min, EHDP was less damaging to enamel surfaces than MA as determined by scanning electron microscopy, grazing angle electron diffraction, and quantitative etch solution analyses. Both MA and EHDP inhibited hydroxyapatite crystal growth, although EHDP was more effective than MA. The formation of a tricalcium mellitate surface phase is suggested as the basis of the MA crystal growth effect on apatite. Both MA and EHDP also inhibited rat calculus formation, but EHDP was more effective than MA. The relation between crystal growth inhibition, surface phase solubility, and anti-calculus activity is discussed and a generalized principal for determining an effective inhibitor of calculus is suggested.
|
An in vitro and in vivo investigation of mellitate and ethane-1-hydroxy-1,1-diphosphonate in calcium phosphate systems. Comparisons of mellitate (MA) and ethane-1-hydroxy-1,1-diphosphonate (EHDP) have been carried out in studies of enamel etching, calcium phosphate crystal growth and animal calculus deposition. In enamel etch studies at pH 5, 6, or 7 and after treatment times of 5 or 170 min, EHDP was less damaging to enamel surfaces than MA as determined by scanning electron microscopy, grazing angle electron diffraction, and quantitative etch solution analyses. Both MA and EHDP inhibited hydroxyapatite crystal growth, although EHDP was more effective than MA. The formation of a tricalcium mellitate surface phase is suggested as the basis of the MA crystal growth effect on apatite. Both MA and EHDP also inhibited rat calculus formation, but EHDP was more effective than MA. The relation between crystal growth inhibition, surface phase solubility, and anti-calculus activity is discussed and a generalized principal for determining an effective inhibitor of calculus is suggested.
|
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] |
PMID:19136
|
Pentose-shunt oxidation in the periosteal cells in healing fractures.
|
The activity of pentose-shunt dehydrogenases is very low in periosteal cells of normal rat metatarsals, but increases one day post-fracture and rises linearly over the next two days. By four days post-fracture, the distribution of this activity along the bone shows two centres of high activity: the first in the region of proliferation to form callus and the second at the site where new bone is first seen, one day later. The high rate of generation of NADPH would be expected to reduce glutathione; reduced glutathione has been shown to inhibit alkaline phosphatase activity in these cells.
|
Pentose-shunt oxidation in the periosteal cells in healing fractures. The activity of pentose-shunt dehydrogenases is very low in periosteal cells of normal rat metatarsals, but increases one day post-fracture and rises linearly over the next two days. By four days post-fracture, the distribution of this activity along the bone shows two centres of high activity: the first in the region of proliferation to form callus and the second at the site where new bone is first seen, one day later. The high rate of generation of NADPH would be expected to reduce glutathione; reduced glutathione has been shown to inhibit alkaline phosphatase activity in these cells.
|
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] |
PMID:19137
|
The inhibition of calcium oxalate crystal growth by multidentate organic phosphonates.
|
The effect of a number of structurally related multidentate organic phosphonates on the rate of crystal growth of calcium oxalate was studied as a function of pH. Rate constants were obtained at various concentrations for the phosphonates ethane-1-hydroxy-1,1-diphosphonate (EHDP), nitrilotri(methylenephosphonic acid) (NTMP), N,N,N',N'-ethylene-diaminetetra(methylenephosphonic acid) (ENTNP), and N,N,N',N'-hexamethylenediaminetetra(methylenephosphonic acid (HMTMP), at pH 5.00, 6.00, and 7.00. The effect of pH on the inhibitory activity of each of the phosphonates was considerable with effective concentrations of inhibitor decreasing two orders of magnitude, in some cases, as the pH was increased. At a given pH the potentially hexadentate ligands, ENTMP and HMTMP, were generally the most effective inhibitors. The results suggested that EHDP, at currently administered doses, provides only a moderate increase in the capacity of human urine to inhibit calcium oxalate crystal growth.
|
The inhibition of calcium oxalate crystal growth by multidentate organic phosphonates. The effect of a number of structurally related multidentate organic phosphonates on the rate of crystal growth of calcium oxalate was studied as a function of pH. Rate constants were obtained at various concentrations for the phosphonates ethane-1-hydroxy-1,1-diphosphonate (EHDP), nitrilotri(methylenephosphonic acid) (NTMP), N,N,N',N'-ethylene-diaminetetra(methylenephosphonic acid) (ENTNP), and N,N,N',N'-hexamethylenediaminetetra(methylenephosphonic acid (HMTMP), at pH 5.00, 6.00, and 7.00. The effect of pH on the inhibitory activity of each of the phosphonates was considerable with effective concentrations of inhibitor decreasing two orders of magnitude, in some cases, as the pH was increased. At a given pH the potentially hexadentate ligands, ENTMP and HMTMP, were generally the most effective inhibitors. The results suggested that EHDP, at currently administered doses, provides only a moderate increase in the capacity of human urine to inhibit calcium oxalate crystal growth.
|
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] |
PMID:19138
|
Comparative toxicities of enflurane, fluroxene and nitrous oxide at subanaesthetic concentrations in laboratory animals.
|
We compared the toxicities of subanesthetic concentrations of fluroxene, enflurane and nitrous oxide in mice, rats and guinea pigs which were in an active growth phase. Fluroxene produced a greater mortality and decrement in weight gain than enflurane and nitrous oxide despite administration of far lower concentrations. Enflurane, 0.1 MAC, resulted in a detrimental effect on weight and early mortality in mice but not in rats or guinea pigs. Nitrous oxide, 0.1 MAC, resulted in only a minor effect on weight gain in guinea pigs and an increased incidence of focal inflammatory liver changes in mice. No consistent injury to any organs other than liver or kidney were found.
|
Comparative toxicities of enflurane, fluroxene and nitrous oxide at subanaesthetic concentrations in laboratory animals. We compared the toxicities of subanesthetic concentrations of fluroxene, enflurane and nitrous oxide in mice, rats and guinea pigs which were in an active growth phase. Fluroxene produced a greater mortality and decrement in weight gain than enflurane and nitrous oxide despite administration of far lower concentrations. Enflurane, 0.1 MAC, resulted in a detrimental effect on weight and early mortality in mice but not in rats or guinea pigs. Nitrous oxide, 0.1 MAC, resulted in only a minor effect on weight gain in guinea pigs and an increased incidence of focal inflammatory liver changes in mice. No consistent injury to any organs other than liver or kidney were found.
|
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] |
PMID:19139
|
Identification of beta adrenergic receptors in rat hypothalamus.
|
(-)-[3H]-Dihydroalprenolol((-)[3H]DHA) binding in the rat hypothalamus appears to possess all the characteristics expected of physiologically relevant beta-adrenergic receptors. Binding of (-)-[3H]DHA to the hypothalamic sites was rapid (k1 = 1.3 X 10(-7) min-1) and also rapidly reversible. Binding was saturable at low concentrations of ligand (approximately 50-100 nM). The dissociation constant (KD) of (-)-[3H]DHA binding determined by equilibrium analysis was 19 nM. Binding displayed beta-adrenergic specificity. beta-Adrenergic agonists inhibited binding in the following order of potency: (-)-isoproterenol congruent to (-)-epinephrine greater than (-)-norepinephrine. Specific beta-adrenergic antagonists (-)-propranol and (-)-alprenolol inhibited binding at low concentrations (KD = 25-50nM) whereas the alpha-antagonist phentolamine inhibited binding at very high concentration (KD = 42 micron). Interactions of both agonists and antagonists with the sites showed stereoselectivity. The (-)-isomers of all beta-adrenergic agents tested were more potent than their respective (+)-isomers. These results suggest that specific receptor sites for beta-adrenergic catecholamines are present in rat hypothalamus.
|
Identification of beta adrenergic receptors in rat hypothalamus. (-)-[3H]-Dihydroalprenolol((-)[3H]DHA) binding in the rat hypothalamus appears to possess all the characteristics expected of physiologically relevant beta-adrenergic receptors. Binding of (-)-[3H]DHA to the hypothalamic sites was rapid (k1 = 1.3 X 10(-7) min-1) and also rapidly reversible. Binding was saturable at low concentrations of ligand (approximately 50-100 nM). The dissociation constant (KD) of (-)-[3H]DHA binding determined by equilibrium analysis was 19 nM. Binding displayed beta-adrenergic specificity. beta-Adrenergic agonists inhibited binding in the following order of potency: (-)-isoproterenol congruent to (-)-epinephrine greater than (-)-norepinephrine. Specific beta-adrenergic antagonists (-)-propranol and (-)-alprenolol inhibited binding at low concentrations (KD = 25-50nM) whereas the alpha-antagonist phentolamine inhibited binding at very high concentration (KD = 42 micron). Interactions of both agonists and antagonists with the sites showed stereoselectivity. The (-)-isomers of all beta-adrenergic agents tested were more potent than their respective (+)-isomers. These results suggest that specific receptor sites for beta-adrenergic catecholamines are present in rat hypothalamus.
|
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] |
PMID:19143
|
Resolution of rat renin substrates by isoelectric focusing.
|
Pooled plasmas from normal or binephrectomized rats and perfusates of isolated livers were used as sources of renin substrate for isoelectric focusing. After desalting, preliminary fractionation (plasma only), and concentration, the preparations were focused in a pH 3--10 gradient on 20-cm glass plates layered with Sephadex slurry. The pH 4--6 region, containing all the substrate, was scraped from this plate and refocused in a pH 4--6 gradient. Substrate content of 1-cm strips of slurry from half of the plate was determined by both radioimmunoassay and bioassay of angiotensin resulting from incubation with added renin. Corresponding strips from the other half of the plate were incubated without renin as a control for any preformed angiotensin. The asymmetry and broad distribution (pH 4--5) of substrate from different sources suggested the existence of more than one form. Higher resolution achieved by using the high substrate concentration of postnephrectomy plasma and 0.5-cm strips of slurry on 20-cm or 40-cm plates revealed peaks and shoulders of substrate activity. Our data suggest that multiple forms of substrate are synthesized by the liver and circulate in plasma. Postnephrectomy rat plasma appears to contain relatively more substrate(s) with higher isoelectric points than in normal plasma, possibly an accumulation of forms ordinarily degraded by endogenous renal renin.
|
Resolution of rat renin substrates by isoelectric focusing. Pooled plasmas from normal or binephrectomized rats and perfusates of isolated livers were used as sources of renin substrate for isoelectric focusing. After desalting, preliminary fractionation (plasma only), and concentration, the preparations were focused in a pH 3--10 gradient on 20-cm glass plates layered with Sephadex slurry. The pH 4--6 region, containing all the substrate, was scraped from this plate and refocused in a pH 4--6 gradient. Substrate content of 1-cm strips of slurry from half of the plate was determined by both radioimmunoassay and bioassay of angiotensin resulting from incubation with added renin. Corresponding strips from the other half of the plate were incubated without renin as a control for any preformed angiotensin. The asymmetry and broad distribution (pH 4--5) of substrate from different sources suggested the existence of more than one form. Higher resolution achieved by using the high substrate concentration of postnephrectomy plasma and 0.5-cm strips of slurry on 20-cm or 40-cm plates revealed peaks and shoulders of substrate activity. Our data suggest that multiple forms of substrate are synthesized by the liver and circulate in plasma. Postnephrectomy rat plasma appears to contain relatively more substrate(s) with higher isoelectric points than in normal plasma, possibly an accumulation of forms ordinarily degraded by endogenous renal renin.
|
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] |
PMID:19144
|
Preparation and galactosyltransferase acceptor activity of derivatives of antifreeze glycoproteins of an Antarctic fish.
|
A series of 12 closely related glycoproteins containing alpha-linked N-acetyl-D-galactosamine (GalNAc) as the sole carbohydrate moiety have been prepared by degradation of the antifreeze glycoproteins from the serum of the Antarctic fish Trematomus borchgrevinki. The polypeptide moieties of these glycoproteins contain substitutions in the normal -Ala-Ala-Thr- repeating tripeptide sequence which introduce alterations in the amount of alpha-helical structure and the density of acceptor sites, and theoretically also in the amount of rigidity, polarity, and hydrophobicity of the polypeptide. Of these alterations only density of acceptor sites has a statistically significant effect on the ability of the GalNAc alpha leads to Thr moiety to act as a substrate for galactosyltransferase (EC 2.4.1.22) activity solubilized from rat liver microsomes. This result suggests that in the biosynthesis of rat liver glycoproteins these structural features of the polypeptide moiety of glycoproteins are not part of the substrate specificity of the galactosyltransferase activity that transfers the second monosaccharide. Hence, these structural features do not play a major role in determining the structure of the threonine-linked oligosaccharide after its synthesis has been initiated.
|
Preparation and galactosyltransferase acceptor activity of derivatives of antifreeze glycoproteins of an Antarctic fish. A series of 12 closely related glycoproteins containing alpha-linked N-acetyl-D-galactosamine (GalNAc) as the sole carbohydrate moiety have been prepared by degradation of the antifreeze glycoproteins from the serum of the Antarctic fish Trematomus borchgrevinki. The polypeptide moieties of these glycoproteins contain substitutions in the normal -Ala-Ala-Thr- repeating tripeptide sequence which introduce alterations in the amount of alpha-helical structure and the density of acceptor sites, and theoretically also in the amount of rigidity, polarity, and hydrophobicity of the polypeptide. Of these alterations only density of acceptor sites has a statistically significant effect on the ability of the GalNAc alpha leads to Thr moiety to act as a substrate for galactosyltransferase (EC 2.4.1.22) activity solubilized from rat liver microsomes. This result suggests that in the biosynthesis of rat liver glycoproteins these structural features of the polypeptide moiety of glycoproteins are not part of the substrate specificity of the galactosyltransferase activity that transfers the second monosaccharide. Hence, these structural features do not play a major role in determining the structure of the threonine-linked oligosaccharide after its synthesis has been initiated.
|
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] |
PMID:19146
|
The role of cyclic nucleotides in the CNS.
|
On the basis of the information presented in this review, it is difficult to reach any firm decision regarding the role of cyclic AMP (or cyclic GMP) in synaptic transmission in the brain. While it is clear that cyclic nucleotide levels can be altered by the exposure of neural tissues to various neurotransmitters, it would be premature to claim that these nucleotides are, or are not, essential to the transmission process in the pre-or post-synaptic components of the synapse. In future experiments with cyclic AMP it will be necessary to consider more critically whether the extracellularly applied nucleotide merely provides a source of adenosine and is thus activating an extracellularly located adenosine receptor, or whether it is actually reaching the hypothetical sites at which it might act as a second messenger. The application of cyclic AMP by intrcellular injection techniques should minimize this particular problem, although possibly at the expense of new diffulties. Prio blockade of the adenosine receptor with agents such as theophylline or adenine xylofuranoside may also assist in the categorization of responses to extracellularly applied cyclic AMP as being a result either of activation of the adenosine receptor or of some other mechanism. Utimately, the developement of highly specific inhibitor for adenylate cyclase should provide a firm basis from which to draw conclusions about the role of cyclic AMP in synaptic transmission. Similar considerations apply to the action of cyclic GMP and the role of its synthesizing enzyme, guanylate cyclase. The use of phosphodiesterase inhibitors in studies on cyclic nucleotides must also be approached with caution. The diverse actions of many of these compounds, which include calcium mobilization and block of adenosine uptake, could account for many of the results that have been reported in the literature.
|
The role of cyclic nucleotides in the CNS. On the basis of the information presented in this review, it is difficult to reach any firm decision regarding the role of cyclic AMP (or cyclic GMP) in synaptic transmission in the brain. While it is clear that cyclic nucleotide levels can be altered by the exposure of neural tissues to various neurotransmitters, it would be premature to claim that these nucleotides are, or are not, essential to the transmission process in the pre-or post-synaptic components of the synapse. In future experiments with cyclic AMP it will be necessary to consider more critically whether the extracellularly applied nucleotide merely provides a source of adenosine and is thus activating an extracellularly located adenosine receptor, or whether it is actually reaching the hypothetical sites at which it might act as a second messenger. The application of cyclic AMP by intrcellular injection techniques should minimize this particular problem, although possibly at the expense of new diffulties. Prio blockade of the adenosine receptor with agents such as theophylline or adenine xylofuranoside may also assist in the categorization of responses to extracellularly applied cyclic AMP as being a result either of activation of the adenosine receptor or of some other mechanism. Utimately, the developement of highly specific inhibitor for adenylate cyclase should provide a firm basis from which to draw conclusions about the role of cyclic AMP in synaptic transmission. Similar considerations apply to the action of cyclic GMP and the role of its synthesizing enzyme, guanylate cyclase. The use of phosphodiesterase inhibitors in studies on cyclic nucleotides must also be approached with caution. The diverse actions of many of these compounds, which include calcium mobilization and block of adenosine uptake, could account for many of the results that have been reported in the literature.
|
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] |
PMID:19147
|
Future of anesthesia.
|
The authors present an account of some of the problems facing the specialty of anesthesia, which suggests that the interdependence of these problems and of their solutions should be recognized. Recruitment, job satisfaction and clinical standards will be improved as a result of greater involvement by anesthetists in preanesthetic care as part of the health care team. Teaching programs require appropriate expansion and modification. The incorporation of a physician-assistant program is essential to the future of anesthesia.
|
Future of anesthesia. The authors present an account of some of the problems facing the specialty of anesthesia, which suggests that the interdependence of these problems and of their solutions should be recognized. Recruitment, job satisfaction and clinical standards will be improved as a result of greater involvement by anesthetists in preanesthetic care as part of the health care team. Teaching programs require appropriate expansion and modification. The incorporation of a physician-assistant program is essential to the future of anesthesia.
|
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] |
PMID:19148
|
The trauma of being psychotic: a neglected element in the management of chronic schizophrenia?
|
A hypothesis is put forward in regards to what is called "chronic schizophrenia" that those observations which suggest a continuing disease process may turn out not to be intrinsic facets of schizophrenia as a neurochemical instability but rather neurotic reactions to the acute schizophrenic process. The hypothesis goes on to suggest that this reaction to the acute psychosis is such as to constitute a traumatic neurosis and that while controlling the psychosis with an "umbrella" of major tranquilizers, it is possible to resolve this neurosis. Resolution of the neurosis requires a particular approach to therapy. This is a hypothesis which is very much open to experimental examination and one which may, if proven, markedly affect the postpsychosis management of schizophrenia.
|
The trauma of being psychotic: a neglected element in the management of chronic schizophrenia? A hypothesis is put forward in regards to what is called "chronic schizophrenia" that those observations which suggest a continuing disease process may turn out not to be intrinsic facets of schizophrenia as a neurochemical instability but rather neurotic reactions to the acute schizophrenic process. The hypothesis goes on to suggest that this reaction to the acute psychosis is such as to constitute a traumatic neurosis and that while controlling the psychosis with an "umbrella" of major tranquilizers, it is possible to resolve this neurosis. Resolution of the neurosis requires a particular approach to therapy. This is a hypothesis which is very much open to experimental examination and one which may, if proven, markedly affect the postpsychosis management of schizophrenia.
|
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] |
PMID:19149
|
Desensitization therapy for body image anxiety.
|
A newly devised therapy technique to desensitize individuals for body image anxiety arising from conversion symptoms and psychophysiologic disorders is outlined. One application involves the projective use of inkblots with high anatomical content which provide a source of visual input to stimulate somatic images in consciousness. When these are activated in a state of relaxation the anxiety content of the pathologic anatomical imagery is reduced. A case history involving desensitization treatment for a psychoneurotic patient's psychophysiologic symptom of premature ejaculation is cited. It is primarily designed to alert interested clinical investigators to this technical innovation in treatment.
|
Desensitization therapy for body image anxiety. A newly devised therapy technique to desensitize individuals for body image anxiety arising from conversion symptoms and psychophysiologic disorders is outlined. One application involves the projective use of inkblots with high anatomical content which provide a source of visual input to stimulate somatic images in consciousness. When these are activated in a state of relaxation the anxiety content of the pathologic anatomical imagery is reduced. A case history involving desensitization treatment for a psychoneurotic patient's psychophysiologic symptom of premature ejaculation is cited. It is primarily designed to alert interested clinical investigators to this technical innovation in treatment.
|
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] |
PMID:19150
|
The ability of enteric bacteria to catalyze the covalent binding of bile acids and cholesterol to DNA and their in ability to metabolize benzo(a)pyrene to a binding product and to known metabolites.
|
The capacity of enteric bacteria (E. coli, Salmonella, Pseudomonas, Shigella and Klebsiella) to catalyze the covalent binding of benzo(a)pyrene (BP), cholic acid, deoxycholic acid and cholesterol was investigated. In general, these bacteria were incapable of activating BP to a covalently bound product with calf thymus DNA. Metabolism studies of BP by fluorometric assay failed to indicate any accumulation of BP-3-hydroxy in the incubation medium. Detailed metabolic investigation with high-pressure liquid chromatography indicated that these bacteria did not produce any known metabolites which are formed by mammalian systems. However, radioactivity was detected in all fractions, suggesting that the bacteria were readily metabolizing BP into smaller molecules for energy and carbon sources. Although the enteric bacteria did not metabolize BP into known metabolites, some were capable of activating cholesterol, cholic acid and deoxycholic acid to covalently bound products with DNA. The binding data with cholesterol and bile acids also suggested that the binding process required NADPH as a cofactor because binding level was rather low without NADPH.
|
The ability of enteric bacteria to catalyze the covalent binding of bile acids and cholesterol to DNA and their in ability to metabolize benzo(a)pyrene to a binding product and to known metabolites. The capacity of enteric bacteria (E. coli, Salmonella, Pseudomonas, Shigella and Klebsiella) to catalyze the covalent binding of benzo(a)pyrene (BP), cholic acid, deoxycholic acid and cholesterol was investigated. In general, these bacteria were incapable of activating BP to a covalently bound product with calf thymus DNA. Metabolism studies of BP by fluorometric assay failed to indicate any accumulation of BP-3-hydroxy in the incubation medium. Detailed metabolic investigation with high-pressure liquid chromatography indicated that these bacteria did not produce any known metabolites which are formed by mammalian systems. However, radioactivity was detected in all fractions, suggesting that the bacteria were readily metabolizing BP into smaller molecules for energy and carbon sources. Although the enteric bacteria did not metabolize BP into known metabolites, some were capable of activating cholesterol, cholic acid and deoxycholic acid to covalently bound products with DNA. The binding data with cholesterol and bile acids also suggested that the binding process required NADPH as a cofactor because binding level was rather low without NADPH.
|
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] |
PMID:19152
|
Beta-adrenoceptor antagonists and the release of creatine phosphokinase from hypoxic heart muscle.
|
The ability of several beta-adrenoceptor antagonists with partial agonist activity (dl-oxprenolol, dl-acebutolol and dl-practolol) to attenuate the release of CPK that occurs during hypoxia (pO2 less than 0.8 kPa [6 MMHg]) has been studied and compared with the protection provided by dl-propranolol. dl-propranolol attenuated the hypoxic-induced release of CPK. The activity resided in the l isomer. dl-oxprenolol, acebutolol, and practolol were either less effective than propranolol in preventing CPK release, or they exacerbated the release. The protective effect of dl-propranolol extended to the hypoxic hyperthyroid heart but not to hearts that were perfused under aerobic (pO2 greater than 80 kPa [600 mmHg]) Ca2+-free conditions.
|
Beta-adrenoceptor antagonists and the release of creatine phosphokinase from hypoxic heart muscle. The ability of several beta-adrenoceptor antagonists with partial agonist activity (dl-oxprenolol, dl-acebutolol and dl-practolol) to attenuate the release of CPK that occurs during hypoxia (pO2 less than 0.8 kPa [6 MMHg]) has been studied and compared with the protection provided by dl-propranolol. dl-propranolol attenuated the hypoxic-induced release of CPK. The activity resided in the l isomer. dl-oxprenolol, acebutolol, and practolol were either less effective than propranolol in preventing CPK release, or they exacerbated the release. The protective effect of dl-propranolol extended to the hypoxic hyperthyroid heart but not to hearts that were perfused under aerobic (pO2 greater than 80 kPa [600 mmHg]) Ca2+-free conditions.
|
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] |
PMID:19154
|
The nature of the rate-limiting step in aniline hydroxylation involving cytochrome p-450 rat liver microsomes.
|
The kinetics of aniline hydroxylation was studied with: (1) rat liver microsomes involving NADPH and O2 (system 1), (2) hepatic microsomes and tert-butylhydroperoxide (system 2) and (3) microsomes and cumyl hydroperoxide (system 3) at 15--37 degrees C. The reactions were characterized by the values of the aniline oxidation rate constants, k2 = V/E0, where E0 is the initial concentration of cytochrome P-450: K 1/2 = 1.60 - 10(8) EXP (-13 400/RT) sec-1, k 2/2 = 1.66 - 10(9) exp (-14 500/RT) sec-1, k 3/2 = 6.83 - 10(9) exp (-15 300/RT) sec-1. The values of delta H0 and delta S0, were calculated and compared for the three systems. The evidence suggests that oxygen insertion into the substrate molecule is the rate-limiting step in the reaction of aniline oxidation for the mentioned systems. The nature of aniline binding to cytochrome P-450 and that of the hydroxylating agent have been discussed.
|
The nature of the rate-limiting step in aniline hydroxylation involving cytochrome p-450 rat liver microsomes. The kinetics of aniline hydroxylation was studied with: (1) rat liver microsomes involving NADPH and O2 (system 1), (2) hepatic microsomes and tert-butylhydroperoxide (system 2) and (3) microsomes and cumyl hydroperoxide (system 3) at 15--37 degrees C. The reactions were characterized by the values of the aniline oxidation rate constants, k2 = V/E0, where E0 is the initial concentration of cytochrome P-450: K 1/2 = 1.60 - 10(8) EXP (-13 400/RT) sec-1, k 2/2 = 1.66 - 10(9) exp (-14 500/RT) sec-1, k 3/2 = 6.83 - 10(9) exp (-15 300/RT) sec-1. The values of delta H0 and delta S0, were calculated and compared for the three systems. The evidence suggests that oxygen insertion into the substrate molecule is the rate-limiting step in the reaction of aniline oxidation for the mentioned systems. The nature of aniline binding to cytochrome P-450 and that of the hydroxylating agent have been discussed.
|
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] |
PMID:19157
|
[Splenogonadal fusion].
|
The authors report of case of splenogonadic fusion in abdominal retention, revising the subject from the aetiopathogenetic and diagnostic point of view. It is emphasized that correct recognition of the lesion can obviate useless orchiectomies, preserving normal function of the testicle at least from the endocrinal standpoint.
|
[Splenogonadal fusion]. The authors report of case of splenogonadic fusion in abdominal retention, revising the subject from the aetiopathogenetic and diagnostic point of view. It is emphasized that correct recognition of the lesion can obviate useless orchiectomies, preserving normal function of the testicle at least from the endocrinal standpoint.
|
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] |
PMID:19160
|
[Properties of chlorotetrolic acid and its ester as possible protein acetylenic reagents].
|
Chlorotetrolic acid and, even better, the corresponding methyl ester react under mild conditions with different functional groups. The relative ease with which the same nucleophile adds to the triple bond and substitutes the chlorine was studied and the stability of the addition products was compared.
|
[Properties of chlorotetrolic acid and its ester as possible protein acetylenic reagents]. Chlorotetrolic acid and, even better, the corresponding methyl ester react under mild conditions with different functional groups. The relative ease with which the same nucleophile adds to the triple bond and substitutes the chlorine was studied and the stability of the addition products was compared.
|
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] |
PMID:19163
|
Nucleotide pyrophosphatase and phosphodiesterase. I. Organ distribution and activities in body fluids.
|
We estimated nucleotide pyrophosphatase and phosphodiesterase I activities in human and rat organs and in body fluids from man and dog. The highest organ activities were found in epididymis, kidney, liver, and intestine. In body fluids, the activity was highest in seminal plasma, followed by intestinal lymph, serum, heart lymph, cerebrospinal fluid, milk, and urine. The ratio nucleotide pyrophosphatase/phosphodiesterase I and the urea resistance of phosphodiesterase I differed among human organs, body fluids, and blood cells. Different isoenzymes probably exist. The activities in serum share several properties with those in several organs--e.g. pH-optimum 9.6-9.8, dependency on Zn2+, and the effects of inhibitors. Phosphodiesterase I in erythrocytes, which has not been described previously, differs from enzyme from other sources by lower pH optimum (8.5), dependency on Mg2+, inhibition by Zn2+, and stimulation by dithiothreitol.
|
Nucleotide pyrophosphatase and phosphodiesterase. I. Organ distribution and activities in body fluids. We estimated nucleotide pyrophosphatase and phosphodiesterase I activities in human and rat organs and in body fluids from man and dog. The highest organ activities were found in epididymis, kidney, liver, and intestine. In body fluids, the activity was highest in seminal plasma, followed by intestinal lymph, serum, heart lymph, cerebrospinal fluid, milk, and urine. The ratio nucleotide pyrophosphatase/phosphodiesterase I and the urea resistance of phosphodiesterase I differed among human organs, body fluids, and blood cells. Different isoenzymes probably exist. The activities in serum share several properties with those in several organs--e.g. pH-optimum 9.6-9.8, dependency on Zn2+, and the effects of inhibitors. Phosphodiesterase I in erythrocytes, which has not been described previously, differs from enzyme from other sources by lower pH optimum (8.5), dependency on Mg2+, inhibition by Zn2+, and stimulation by dithiothreitol.
|
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