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PMID:5029 | [Studies of the variations in functional renal values induced by intravenous dopamine]. | We studied, on six patients, the variations in functional renal value and urinary excretion of electrolytes during the intravenous administration of dopamine and in the hours immediately following. Two groups of patients are distinguished. In groupe I, all of whom had normal functional renal values, there was no modification of these, while we observed increases in output, in excretion of electrolytes and in the clearance of the uric acid. In group II, composed of patients with renal insufficiencies, the modifications are less definite but the diuretic and saluretic effect is present. The salidiuretic effects of the dopamine would seem to be dissociated from the cardiovascular effects. | [Studies of the variations in functional renal values induced by intravenous dopamine]. We studied, on six patients, the variations in functional renal value and urinary excretion of electrolytes during the intravenous administration of dopamine and in the hours immediately following. Two groups of patients are distinguished. In groupe I, all of whom had normal functional renal values, there was no modification of these, while we observed increases in output, in excretion of electrolytes and in the clearance of the uric acid. In group II, composed of patients with renal insufficiencies, the modifications are less definite but the diuretic and saluretic effect is present. The salidiuretic effects of the dopamine would seem to be dissociated from the cardiovascular effects. | [
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PMID:5030 | [The use of dopamine during postoperative cardiogenic shock in children. Preliminary results]. | Dopamine was used in a dose of 5 mug/kg/min in ten infants with congenital cardiopathy and presenting in the immediate postoperative period a syndrome of low cardiac output. The output was not measured but, based on the evolution of the clinical signs, six favourable results, with correction of the syndrome, can be reported. | [The use of dopamine during postoperative cardiogenic shock in children. Preliminary results]. Dopamine was used in a dose of 5 mug/kg/min in ten infants with congenital cardiopathy and presenting in the immediate postoperative period a syndrome of low cardiac output. The output was not measured but, based on the evolution of the clinical signs, six favourable results, with correction of the syndrome, can be reported. | [
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PMID:5031 | [Use of dopamine in postoperative reanimation after heart surgery. Preliminary results]. | The dopamine was used on ten patients having undergone one or several valvular replacements under extra-corporeal circulation. The essential indication was the appearance postoperatively of more or less serious circulatory failure. The dopamine was administered by drip in doses of 2.5, 5 or 10 mug/kg/min. The effects on the frequency of the cardiac rhythm were moderate. On two cases, ventricular hyperexcitability induced by isoprenaline disappeared under dopamine. The chief effects were an increase in cardiac output, in the form of an increase in the volume of systolic ejection and lowering of the peripheral resistances. A steady increase in urinary volume preceded the amelioration of clinical signs of circulatory failure. | [Use of dopamine in postoperative reanimation after heart surgery. Preliminary results]. The dopamine was used on ten patients having undergone one or several valvular replacements under extra-corporeal circulation. The essential indication was the appearance postoperatively of more or less serious circulatory failure. The dopamine was administered by drip in doses of 2.5, 5 or 10 mug/kg/min. The effects on the frequency of the cardiac rhythm were moderate. On two cases, ventricular hyperexcitability induced by isoprenaline disappeared under dopamine. The chief effects were an increase in cardiac output, in the form of an increase in the volume of systolic ejection and lowering of the peripheral resistances. A steady increase in urinary volume preceded the amelioration of clinical signs of circulatory failure. | [
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] |
PMID:5032 | [Use of dopamine in acute cardiovascular distress. Its place in comparison to isoproterenol]. | Nineteen patients presenting cardiovascular distress were treated with dopamine. For seventeen of these, the accident occurred immediately after cardiac surgery. Dosages varied from 1 to 15 mug/kg/min and the duration of treatment from 10 minutes to three days. The efficacy of the treatment was judged according to the clinical and hemodynamic improvement of the cardio-circulatory function and the increase in urinary output. There were 15 favourable results. The positive effects of the dopamine seem to be limited in certain patients by the appearance of a cyanosis testifying to a rise in vascular resistances which increases the left auricular pressure and limits the inotropic effect. In these cases, isoproterenol or a combination of both isoproterenol and dopamine gives better results. | [Use of dopamine in acute cardiovascular distress. Its place in comparison to isoproterenol]. Nineteen patients presenting cardiovascular distress were treated with dopamine. For seventeen of these, the accident occurred immediately after cardiac surgery. Dosages varied from 1 to 15 mug/kg/min and the duration of treatment from 10 minutes to three days. The efficacy of the treatment was judged according to the clinical and hemodynamic improvement of the cardio-circulatory function and the increase in urinary output. There were 15 favourable results. The positive effects of the dopamine seem to be limited in certain patients by the appearance of a cyanosis testifying to a rise in vascular resistances which increases the left auricular pressure and limits the inotropic effect. In these cases, isoproterenol or a combination of both isoproterenol and dopamine gives better results. | [
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PMID:5033 | [Dopamine and shock. Preliminary clinical study of 7 cases]. | Seven patients presenting a state of shock were treated with dopamine. The authors remark an undeniable effect on arterial pressure which rises again and on the diuresis. | [Dopamine and shock. Preliminary clinical study of 7 cases]. Seven patients presenting a state of shock were treated with dopamine. The authors remark an undeniable effect on arterial pressure which rises again and on the diuresis. | [
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PMID:5034 | [Use of dopamine in the treatment of cardiogenic shock. Preliminary results]. | A study of seven patients, each of whom was treated with dopamine within three hours after suffering a myocardial infarction. For four of these, a comparative study was made with isoproterenol, glucagon and ouabaine. The average age of the subjects was 72 years, and all presented considerable myocardial lesions before the treatment was begun. Despite improvement, particularly in diuresis and cardiac output, none of the patients survived. The authors explain these results by the fact that, like all powerful inotropic agents, dopamine produces an increase in oxygen consumption of the myocardium for the ischemic cells situated in the zone contiguous to the infarct. | [Use of dopamine in the treatment of cardiogenic shock. Preliminary results]. A study of seven patients, each of whom was treated with dopamine within three hours after suffering a myocardial infarction. For four of these, a comparative study was made with isoproterenol, glucagon and ouabaine. The average age of the subjects was 72 years, and all presented considerable myocardial lesions before the treatment was begun. Despite improvement, particularly in diuresis and cardiac output, none of the patients survived. The authors explain these results by the fact that, like all powerful inotropic agents, dopamine produces an increase in oxygen consumption of the myocardium for the ischemic cells situated in the zone contiguous to the infarct. | [
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PMID:5035 | [Comparison of the endocrine response under 2 kinds of anesthesia: neuroleptanalgesia of the chlorprothixene-dextromoramide type and venous anesthesia of the type alfadione-fentanyl]. | In 14 patients anaesthetized before undergoing an orthopedic surgical intervention, the variations induced by anaesthesia in the 17 hydroxycorticosterone rate, catecholamine, somatotropic hormone (STH), insulin, glycemia, free fatty acids and thyrotropin (TSH), all these variations were studied before the surgery. The patients were divided into 2 groups of 7, the first one being anaesthestized by chlorprothixene dextromoramide Neurolept-Analgesia and the second one by Alfadione Fentanyl venous anaesthesia. | [Comparison of the endocrine response under 2 kinds of anesthesia: neuroleptanalgesia of the chlorprothixene-dextromoramide type and venous anesthesia of the type alfadione-fentanyl]. In 14 patients anaesthetized before undergoing an orthopedic surgical intervention, the variations induced by anaesthesia in the 17 hydroxycorticosterone rate, catecholamine, somatotropic hormone (STH), insulin, glycemia, free fatty acids and thyrotropin (TSH), all these variations were studied before the surgery. The patients were divided into 2 groups of 7, the first one being anaesthestized by chlorprothixene dextromoramide Neurolept-Analgesia and the second one by Alfadione Fentanyl venous anaesthesia. | [
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PMID:5036 | [The place of enflurane in neuro-anesthesia]. | In neuro-anaesthesia, anaesthetic agents must be in accordance with certain criteria necessary to the preservation of the integrity of the brain. Therefore it was in such a perspective that we re-appraised the effects of enflurane upon cortical irritability, metabolism, cerebral blood flow and intracranial pressure. We reached the following conclusions: in normocapnia, and with optimal clinical concentrations, this drug remains the best anaesthetic agent since it has no harmful effect either upon metabolism or upon cerebral blood flow. However, in hypertensive cerebral lesions, caution is called for an it seems advisable to combine Enflurane with mild doses of fentanyl. Finally, anaesthesia with enflurane is followed by a rapid and smooth return to consciousness, a valuable factor in neurosurgery where post-operative neurological watching matters very much. | [The place of enflurane in neuro-anesthesia]. In neuro-anaesthesia, anaesthetic agents must be in accordance with certain criteria necessary to the preservation of the integrity of the brain. Therefore it was in such a perspective that we re-appraised the effects of enflurane upon cortical irritability, metabolism, cerebral blood flow and intracranial pressure. We reached the following conclusions: in normocapnia, and with optimal clinical concentrations, this drug remains the best anaesthetic agent since it has no harmful effect either upon metabolism or upon cerebral blood flow. However, in hypertensive cerebral lesions, caution is called for an it seems advisable to combine Enflurane with mild doses of fentanyl. Finally, anaesthesia with enflurane is followed by a rapid and smooth return to consciousness, a valuable factor in neurosurgery where post-operative neurological watching matters very much. | [
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PMID:5039 | Immunology and microbiology in acute otitis media. | Various immunological parameters were measured in serum, middle ear fluid (MEF), and lymphocytes from peripheral blood and MEF of infants with acute otitis media due to S. pneumoniae or H. influenzae. Approximately half of 131 patients had IgE specific antibody to the infecting bacterium as determined by the indirect fluorescent antibody (IFA) technique. Seventy-one percent of these IgE positive patients had IgE specific antibody in the MEF. Total IgE concentration was found to be from an average of 1.5 to 3.0 times higher in the MEF when compared to the simultaneously drawn serum. In addition, antibody to pneumococcal capsular polysaccharides and to pneumococcal C-carbohydrate was demonstrated in the MEF by radioimmunoassay. When MEF specific antibody was compared to serum antibody it appeared that antibody to C-carbohydrate was more concentrated in the MEF. That this antibody was of the IgE class was suggested by IFA but not conclusively proven. Evidence exists that conditions for enhanced IgE synthesis is concomitantly associated with a decrease in T-cell activity. T-cell function in MEF derived lymphocytes as determined by rosette formation and by phytohemagglutinin (PHA) stimulation was approximately one-tenth that of the peripheral blood lymphocytes. However, that T-cells may participate in the immune response to polysaccharides was suggested by the observation that polysaccharide stimulated peripheral blood lymphocytes from infants immunized with octavalent pneumococcal capsular vaccine underwent protein synthesis two to three times that of the PHA stimulated cells. The clinical significance of this finding as well as the nature of the cell responsible for the increased protein synthesis remains to be established. It is hypothesized that acute otitis media results from local synthesis of bacteria specific IgE antibody which is enhanced by a paucity of local T-cell activity. | Immunology and microbiology in acute otitis media. Various immunological parameters were measured in serum, middle ear fluid (MEF), and lymphocytes from peripheral blood and MEF of infants with acute otitis media due to S. pneumoniae or H. influenzae. Approximately half of 131 patients had IgE specific antibody to the infecting bacterium as determined by the indirect fluorescent antibody (IFA) technique. Seventy-one percent of these IgE positive patients had IgE specific antibody in the MEF. Total IgE concentration was found to be from an average of 1.5 to 3.0 times higher in the MEF when compared to the simultaneously drawn serum. In addition, antibody to pneumococcal capsular polysaccharides and to pneumococcal C-carbohydrate was demonstrated in the MEF by radioimmunoassay. When MEF specific antibody was compared to serum antibody it appeared that antibody to C-carbohydrate was more concentrated in the MEF. That this antibody was of the IgE class was suggested by IFA but not conclusively proven. Evidence exists that conditions for enhanced IgE synthesis is concomitantly associated with a decrease in T-cell activity. T-cell function in MEF derived lymphocytes as determined by rosette formation and by phytohemagglutinin (PHA) stimulation was approximately one-tenth that of the peripheral blood lymphocytes. However, that T-cells may participate in the immune response to polysaccharides was suggested by the observation that polysaccharide stimulated peripheral blood lymphocytes from infants immunized with octavalent pneumococcal capsular vaccine underwent protein synthesis two to three times that of the PHA stimulated cells. The clinical significance of this finding as well as the nature of the cell responsible for the increased protein synthesis remains to be established. It is hypothesized that acute otitis media results from local synthesis of bacteria specific IgE antibody which is enhanced by a paucity of local T-cell activity. | [
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PMID:5040 | Otitis media in the newborn infant. | Otitis media occurs frequently in newborn infants and often is associated with systemic infection. Patients studied at the Boston City Hospital have provided preliminary data on the otoscopic findings, tympanometric patterns and etiologic agents characteristic of otitis in this age group. | Otitis media in the newborn infant. Otitis media occurs frequently in newborn infants and often is associated with systemic infection. Patients studied at the Boston City Hospital have provided preliminary data on the otoscopic findings, tympanometric patterns and etiologic agents characteristic of otitis in this age group. | [
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PMID:5041 | Microorganisms in chronic otitis media with effusion. | A total of 175 effusions obtained from 172 patients suffering from chronic otitis media with effusions was examined for bacterial smear and culture. Eighty percent showed positive bacterial smear, but only 49% yielded positive bacterial culture. The mucoid effusions had positive cultures in only 37%, whereas the bacterial culture rate was higher in serous (59%) and leukocytic (64%) types. The isolation of common pathogens accounted for about 50% of the isolates, and nonpathogens accounted for the remaining 50%. The high incidence of microorganisms in the middle ear effusions in the present series raises the possibility of bacterial contribution in many cases of OME. | Microorganisms in chronic otitis media with effusion. A total of 175 effusions obtained from 172 patients suffering from chronic otitis media with effusions was examined for bacterial smear and culture. Eighty percent showed positive bacterial smear, but only 49% yielded positive bacterial culture. The mucoid effusions had positive cultures in only 37%, whereas the bacterial culture rate was higher in serous (59%) and leukocytic (64%) types. The isolation of common pathogens accounted for about 50% of the isolates, and nonpathogens accounted for the remaining 50%. The high incidence of microorganisms in the middle ear effusions in the present series raises the possibility of bacterial contribution in many cases of OME. | [
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PMID:5044 | Gastro-oesophageal reflux and hiatal hernia. A re-evaluation of current data and dogma. | Various methods of investigating and treating patients with gastro-oesophageal disorders are described and the rationale of current concepts is outlined. Emphasis is placed throughout on gastro-oesophageal reflux and its sequelae rather than on sliding hiatal hernias. Symptoms of gastro-oesophageal dysfunction can be misleading, and careful studies are essential in assessing its importance and the results of various modes of therapy. | Gastro-oesophageal reflux and hiatal hernia. A re-evaluation of current data and dogma. Various methods of investigating and treating patients with gastro-oesophageal disorders are described and the rationale of current concepts is outlined. Emphasis is placed throughout on gastro-oesophageal reflux and its sequelae rather than on sliding hiatal hernias. Symptoms of gastro-oesophageal dysfunction can be misleading, and careful studies are essential in assessing its importance and the results of various modes of therapy. | [
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PMID:5046 | A new look at the measurement and interpretation of enzyme assays. | Some methodological problems in clinical enzymology, including instability of enzymes in the incubation mixture and requirements for optimal reaction conditions, are highlighted. The importance of a knowledge of fundamental enzyme biochemistry and physiology as the basis for their diagnostic application is stressed, and the different behaviour of some hepatic enzymes--namely, GOT, GPT, gamma-GT, and OCT, in various pathological conditions is traced back to their characteristic biochemical and physiological properties. In the field of urinary enzymes a knowledge of the ideal requirements for the enzyme investigation of the various renal functions and of the properties of potentially valuable enzymes permits a critical selection of the really useful ones. | A new look at the measurement and interpretation of enzyme assays. Some methodological problems in clinical enzymology, including instability of enzymes in the incubation mixture and requirements for optimal reaction conditions, are highlighted. The importance of a knowledge of fundamental enzyme biochemistry and physiology as the basis for their diagnostic application is stressed, and the different behaviour of some hepatic enzymes--namely, GOT, GPT, gamma-GT, and OCT, in various pathological conditions is traced back to their characteristic biochemical and physiological properties. In the field of urinary enzymes a knowledge of the ideal requirements for the enzyme investigation of the various renal functions and of the properties of potentially valuable enzymes permits a critical selection of the really useful ones. | [
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PMID:5043 | Allergic factors in management of middle ear effusions. | There is no single specific therapy for the treatment of middle ear effusions and, therefore, a holistic approach to management is necessary. Current management involves multiple therapeutic modalities of which we believe tube and allergy are most efficient. | Allergic factors in management of middle ear effusions. There is no single specific therapy for the treatment of middle ear effusions and, therefore, a holistic approach to management is necessary. Current management involves multiple therapeutic modalities of which we believe tube and allergy are most efficient. | [
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PMID:5047 | [Properties of penicillin amidase covalently bound to cellulose matrices]. | Properties of penicillinamidase (PA) covalently bound with the cellulose matrix were studied. The efficiency of the binding depended on the bind type and purity of the native enzyme taken for binding. Stability of the immobilized PA (IPA) was studied at wide pH ranges. The effect of the ion strength, substrate concentration and purity of the native PA on stability of IPA was also investigated. The maximum stability of the enzyme was observed at pH 6.5-7.0 Stability of IPA depended on the purity of the native enzyme. When PA of the diazotized ether of cellulose containing amino groups was used, the enzyme was destabilized. IPA prepared on chlortriazinylcellulose was more stable than the respective native PA almost by I order. | [Properties of penicillin amidase covalently bound to cellulose matrices]. Properties of penicillinamidase (PA) covalently bound with the cellulose matrix were studied. The efficiency of the binding depended on the bind type and purity of the native enzyme taken for binding. Stability of the immobilized PA (IPA) was studied at wide pH ranges. The effect of the ion strength, substrate concentration and purity of the native PA on stability of IPA was also investigated. The maximum stability of the enzyme was observed at pH 6.5-7.0 Stability of IPA depended on the purity of the native enzyme. When PA of the diazotized ether of cellulose containing amino groups was used, the enzyme was destabilized. IPA prepared on chlortriazinylcellulose was more stable than the respective native PA almost by I order. | [
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PMID:5048 | [Determination of the biological activity of heliomycin by a method of diffusion in agar]. | A biological method for determination of geliomycin activity using agar diffusion is described. A nutrient medium containing Hottinger broth up to 35 mg per cent of amine nitrogen, 1.5 percent of agar-agar, tap water, pH 7.8 to 8.0 was used. Bacillus subtilis ATCC 6633 served as the test-culture. Geliomycin was dissolved in 0.1 N sodium hydroxide solution. | [Determination of the biological activity of heliomycin by a method of diffusion in agar]. A biological method for determination of geliomycin activity using agar diffusion is described. A nutrient medium containing Hottinger broth up to 35 mg per cent of amine nitrogen, 1.5 percent of agar-agar, tap water, pH 7.8 to 8.0 was used. Bacillus subtilis ATCC 6633 served as the test-culture. Geliomycin was dissolved in 0.1 N sodium hydroxide solution. | [
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PMID:5049 | [Study of the effect of the oxytetracycline crystallization conditions on the process indices]. | Such factors as the rate of the changes in pH, temperature, mixer speed and the nature of the anions present in the solution has a significant effect on the indices of oxytetracycline dihydrate crystallization, i. e. residual content of the antibiotic in the mother solution and the specific surface of the crystalls. In this connection the effect of the above factors on the main indices of the process were studied. On the basis of the experimental data dependences were found which provided determination of the crystallization conditions securing the process indices. | [Study of the effect of the oxytetracycline crystallization conditions on the process indices]. Such factors as the rate of the changes in pH, temperature, mixer speed and the nature of the anions present in the solution has a significant effect on the indices of oxytetracycline dihydrate crystallization, i. e. residual content of the antibiotic in the mother solution and the specific surface of the crystalls. In this connection the effect of the above factors on the main indices of the process were studied. On the basis of the experimental data dependences were found which provided determination of the crystallization conditions securing the process indices. | [
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] |
PMID:5050 | [Analysis of the data in the literature on the sensitivity of cholera vibrios to tetracycline]. | Variation diagrams were proposed to be used for the analysis of the published data on the study of Vibrio cholerae sensitivity to tetracycline. The diagrams provided systematization of dissimilar data of the experimental studies and a unique system of estimation was created. The analysis of the systematized data provided dividing of the Vibrio cholerae strains tested into 4 groups differing in the levels of their sensitivity to tetracycline. The groups were independent of the Vibrio cholerae biotypes and the place and period of the strain isolation. | [Analysis of the data in the literature on the sensitivity of cholera vibrios to tetracycline]. Variation diagrams were proposed to be used for the analysis of the published data on the study of Vibrio cholerae sensitivity to tetracycline. The diagrams provided systematization of dissimilar data of the experimental studies and a unique system of estimation was created. The analysis of the systematized data provided dividing of the Vibrio cholerae strains tested into 4 groups differing in the levels of their sensitivity to tetracycline. The groups were independent of the Vibrio cholerae biotypes and the place and period of the strain isolation. | [
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PMID:5051 | [Toxicological characteristics of ampicillin]. | Toxocity of ampicillin trihydrate was studied in acute and chronic experiments. It was shown that the antibiotic had low acute toxicity, did not cumulate and had no skin-irritating effect. On its inhalation in concentrations of 5 mg/m3 for 4 months, ampicillin induced allergization of albino rats, decreased their immunity. The general toxic effect of the drug was slightly pronounced. Ampicillin in a concentration of 0.1 mg/m3 induced tension of the immunological reactivity of the organism. The maximum permissible concentration (MPC) of ampicillin in the working premises equal to 0.1 mg/m3 is recommended. Mark "Allergen" is necessary. | [Toxicological characteristics of ampicillin]. Toxocity of ampicillin trihydrate was studied in acute and chronic experiments. It was shown that the antibiotic had low acute toxicity, did not cumulate and had no skin-irritating effect. On its inhalation in concentrations of 5 mg/m3 for 4 months, ampicillin induced allergization of albino rats, decreased their immunity. The general toxic effect of the drug was slightly pronounced. Ampicillin in a concentration of 0.1 mg/m3 induced tension of the immunological reactivity of the organism. The maximum permissible concentration (MPC) of ampicillin in the working premises equal to 0.1 mg/m3 is recommended. Mark "Allergen" is necessary. | [
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PMID:5052 | Susceptibility of pneumococci and Haemophilus influenzae to antibacterial agents. | Strains of Diplococcus pneumoniae and Haemophilus influenzae were tested for susceptibility to numerous antibiotics by a twofold agar dilution method using an inocula replicator. Undiluted, fully grown broth cultures were used as inocula for both species, and cultures of pneumococci diluted 1:1,000 were also tested. The antibiotics included most of those in common use in the United States as well as some chemical modifications recently approved and others that are under investigation. The most striking aspect of the results was the marked susceptibility of the pneumococci to all the antibiotics tested except the polymyxins and most of the aminoglycoside antibiotics, although some new aminoglycosides were active in quite low concentrations. Some of the strains of pneumococci were of decreased susceptibility to penicillin G (minimal inhibitory concentrations, 0.2 to 0.4 mug/ml), but none were tetracycline resistant, although such strains had been reported previously from this laboratory. The strains of H. influenzae, which were all serologically nontypable, exhibited different patterns of susceptibility to the groups of antibiotics and to the individual chemically related ones. None of these strains (isolated early in 1972) were ampicillin resistant. The most active agents against H. influenzae were: carbenicillin and ampicillin, analogues related to each of them, rifampin, chloramphenicol, and the polymyxins. However, the tetracycline analogues other than tetracycline, some aminoglycosides, notably tobramycin, kanamycin, gentamicin, and verdamicin, erythromycin, and some new lincomycin analogues were also active in low concentrations. Trimethoprim alone was highly active, and in combination with sulfamethoxazole it was even more active and synergistic against strains of both D. pneumoniae and H. influenzae. | Susceptibility of pneumococci and Haemophilus influenzae to antibacterial agents. Strains of Diplococcus pneumoniae and Haemophilus influenzae were tested for susceptibility to numerous antibiotics by a twofold agar dilution method using an inocula replicator. Undiluted, fully grown broth cultures were used as inocula for both species, and cultures of pneumococci diluted 1:1,000 were also tested. The antibiotics included most of those in common use in the United States as well as some chemical modifications recently approved and others that are under investigation. The most striking aspect of the results was the marked susceptibility of the pneumococci to all the antibiotics tested except the polymyxins and most of the aminoglycoside antibiotics, although some new aminoglycosides were active in quite low concentrations. Some of the strains of pneumococci were of decreased susceptibility to penicillin G (minimal inhibitory concentrations, 0.2 to 0.4 mug/ml), but none were tetracycline resistant, although such strains had been reported previously from this laboratory. The strains of H. influenzae, which were all serologically nontypable, exhibited different patterns of susceptibility to the groups of antibiotics and to the individual chemically related ones. None of these strains (isolated early in 1972) were ampicillin resistant. The most active agents against H. influenzae were: carbenicillin and ampicillin, analogues related to each of them, rifampin, chloramphenicol, and the polymyxins. However, the tetracycline analogues other than tetracycline, some aminoglycosides, notably tobramycin, kanamycin, gentamicin, and verdamicin, erythromycin, and some new lincomycin analogues were also active in low concentrations. Trimethoprim alone was highly active, and in combination with sulfamethoxazole it was even more active and synergistic against strains of both D. pneumoniae and H. influenzae. | [
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PMID:5053 | Comparative incidence of phlebitis due to buffered cephalothin, cephapirin, and cefamandole. | Buffered cephalothin, cefamandole, and cephapirin were compared with respect to their tendency to produce phlebitis. Two grams of each agent was administered every 6 h for 4 days to 12 healthy volunteers in a double-blind crossover fashion. Approximately 50% of intravenous sites developed mild (grade 1) phlebitis and 25% developed moderate (grade 2) phlebitis. The frequency of grade 1 inflammation did not differ significantly among the three cephalosporins. The proportion of individuals eventually exhibiting grade 2 phelebitis was highest with cefamandole, lowest with cephalothin (P = 0.07), and intermediate with cephapirin; however, cephapirin required a substantially greater number of doses to produce grade 2 phelebitis than did the other two drugs. These findings, together with the results of other reports, suggest that interpretation of the phlebitogenic potential of these antibiotics must be made with caution. | Comparative incidence of phlebitis due to buffered cephalothin, cephapirin, and cefamandole. Buffered cephalothin, cefamandole, and cephapirin were compared with respect to their tendency to produce phlebitis. Two grams of each agent was administered every 6 h for 4 days to 12 healthy volunteers in a double-blind crossover fashion. Approximately 50% of intravenous sites developed mild (grade 1) phlebitis and 25% developed moderate (grade 2) phlebitis. The frequency of grade 1 inflammation did not differ significantly among the three cephalosporins. The proportion of individuals eventually exhibiting grade 2 phelebitis was highest with cefamandole, lowest with cephalothin (P = 0.07), and intermediate with cephapirin; however, cephapirin required a substantially greater number of doses to produce grade 2 phelebitis than did the other two drugs. These findings, together with the results of other reports, suggest that interpretation of the phlebitogenic potential of these antibiotics must be made with caution. | [
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PMID:5054 | Citric acid metabolism in hetero- and homofermentative lactic acid bacteria. | The effect of citrate on production of diacetyl and acetoin by four strains each of heterofermentative and homofermentative lactic acid bacteria capable of utilizing citrate was studied. Acetoin was quantitatively the more important compound. The heterofermentative bacteria produced no acetoin or diacetyl in the absence of citrate, and two strains produced traces of acetoin in its presence. Citrate stimulated the growth rate of the heterofermentative lactobacilli. Acidification of all heterofermentative cultures with citric acid resulted in acetoin production. Destruction of accumulated acetoin appeared to coincide with the disappearance of citrate. All homofermentative bacteria produced more acetoin and diacetyl in the presence of citrate than in its absence. Citrate utilization was begun immediately by the streptococci but was delayed until at least the middle of the exponential phase in the case of the lactobacilli. | Citric acid metabolism in hetero- and homofermentative lactic acid bacteria. The effect of citrate on production of diacetyl and acetoin by four strains each of heterofermentative and homofermentative lactic acid bacteria capable of utilizing citrate was studied. Acetoin was quantitatively the more important compound. The heterofermentative bacteria produced no acetoin or diacetyl in the absence of citrate, and two strains produced traces of acetoin in its presence. Citrate stimulated the growth rate of the heterofermentative lactobacilli. Acidification of all heterofermentative cultures with citric acid resulted in acetoin production. Destruction of accumulated acetoin appeared to coincide with the disappearance of citrate. All homofermentative bacteria produced more acetoin and diacetyl in the presence of citrate than in its absence. Citrate utilization was begun immediately by the streptococci but was delayed until at least the middle of the exponential phase in the case of the lactobacilli. | [
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PMID:5055 | Influence of specific growth rate on biomass yield, productivity, and compostion of Candida utilis in batch and continuous culture. | Candida utilis was grown in batch and continuous culture on prickly pear juice as sole carbon and energy source. In batch culture the maximum specific growth rate (mum) and the substrate yield coefficient (Yps) varied according to sugar concentration. When the fermentation was carried out with 1% sugar, mum and Ys were 0.47/h and 42.6%, respectively. The best yields occurred in a chemostat at the pH range of 3.5 to 4.5 and temperature of 30 C. A beneficial effect on Ys was observed when the dilution rate (D) was increased. At a D of 0.55/h, the productivity was 2.38 g/liter per h. The maintenance coefficient attained a value of 0.09 g of sugar/g of biomass per h. Increases of D produced higher protein contents of the biomass. The information obtained indicates that protein production with Candida utilis, using prickly pear juice, should be carried out a high dilution rates where the Ys and protein content of the cell mass are also higher. | Influence of specific growth rate on biomass yield, productivity, and compostion of Candida utilis in batch and continuous culture. Candida utilis was grown in batch and continuous culture on prickly pear juice as sole carbon and energy source. In batch culture the maximum specific growth rate (mum) and the substrate yield coefficient (Yps) varied according to sugar concentration. When the fermentation was carried out with 1% sugar, mum and Ys were 0.47/h and 42.6%, respectively. The best yields occurred in a chemostat at the pH range of 3.5 to 4.5 and temperature of 30 C. A beneficial effect on Ys was observed when the dilution rate (D) was increased. At a D of 0.55/h, the productivity was 2.38 g/liter per h. The maintenance coefficient attained a value of 0.09 g of sugar/g of biomass per h. Increases of D produced higher protein contents of the biomass. The information obtained indicates that protein production with Candida utilis, using prickly pear juice, should be carried out a high dilution rates where the Ys and protein content of the cell mass are also higher. | [
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PMID:5056 | Chemical manipulation of the heat resistance of Clostridium botulinum spores. | The chemical forms of Clostridium botulinum 62A and 213B were prepared, and their heat resistances were determined in several heating media, including some low-acid foods. The heat resistance of C. botulinum spores can be manipulated up and down by changing chemical forms between the resistant calcium form and the sensitive hydrogen form. The resistant chemical form of type B spores has about three times the classical PO4 resistance at 235 F (112.8 C). As measured in peas and asparagus, both types of C. botulinum spores came directly from the culture at only a small fraction of the potential heat resistance shown by the same spores when chemically converted to the resistant form. The resistant spore form of both types (62A and 213B), when present in a low-acid food, can be sensitized to heating at the normal pH of the food. | Chemical manipulation of the heat resistance of Clostridium botulinum spores. The chemical forms of Clostridium botulinum 62A and 213B were prepared, and their heat resistances were determined in several heating media, including some low-acid foods. The heat resistance of C. botulinum spores can be manipulated up and down by changing chemical forms between the resistant calcium form and the sensitive hydrogen form. The resistant chemical form of type B spores has about three times the classical PO4 resistance at 235 F (112.8 C). As measured in peas and asparagus, both types of C. botulinum spores came directly from the culture at only a small fraction of the potential heat resistance shown by the same spores when chemically converted to the resistant form. The resistant spore form of both types (62A and 213B), when present in a low-acid food, can be sensitized to heating at the normal pH of the food. | [
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PMID:5057 | Poliovirus survival and movement in a sandy forest soil. | Movement of poliovirus I (Chat) through nonsterile core samples of a sandy forest soil was monitored, using several regimens of loading with either dechlorinated final effluent from an operating activated sludge treatment plant or distilled water. Stimulated cycles of rainfall and effluent applications, resulting in ionic gradients, were shown to affect virus movement. Such studies indicate that poliovirus applied in effluents may move considerable distances through this soil after rainfall. Survival of poliovirus in the soil at 4 and 20 C has been monitored for 84 days. During this period, the capacity of the virus to migrate is unchanged. | Poliovirus survival and movement in a sandy forest soil. Movement of poliovirus I (Chat) through nonsterile core samples of a sandy forest soil was monitored, using several regimens of loading with either dechlorinated final effluent from an operating activated sludge treatment plant or distilled water. Stimulated cycles of rainfall and effluent applications, resulting in ionic gradients, were shown to affect virus movement. Such studies indicate that poliovirus applied in effluents may move considerable distances through this soil after rainfall. Survival of poliovirus in the soil at 4 and 20 C has been monitored for 84 days. During this period, the capacity of the virus to migrate is unchanged. | [
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PMID:5058 | Surface balance study of the interaction between microorganisms and lipid monolayer at the air/water interface. | Using the surface balance technique, we have compared the interaction between Acholeplasma laidlawii and some marine bacteria towards different types of monolayered lipid films. Cells from A. laidlawii and Serratia marinorubra penetrate the film, whereas cells from Psuedomonas fluorescens form a layer underneath the film. The forces that bind microorganisms to the air/water interface are not strong enough to scatter a condensed monolayer but increase the strength of loosely packed monolayers. | Surface balance study of the interaction between microorganisms and lipid monolayer at the air/water interface. Using the surface balance technique, we have compared the interaction between Acholeplasma laidlawii and some marine bacteria towards different types of monolayered lipid films. Cells from A. laidlawii and Serratia marinorubra penetrate the film, whereas cells from Psuedomonas fluorescens form a layer underneath the film. The forces that bind microorganisms to the air/water interface are not strong enough to scatter a condensed monolayer but increase the strength of loosely packed monolayers. | [
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PMID:5059 | Toxicity of natural pyrethrins and five pyrethroids to fish. | The toxicity of natural pyrethrins and five pyrethroids was determined with coho salmon (Oncorhynchus kisutch), steelhead trout (Salmo gairdneri), fathead minnow (Pimephales promelas), channel catfish (Icatlurus punctatus), bluegill (Lepomis macrochirus), and yellow perch (Perca flavescens). The 96-hour LC50's in static tests at 12 degrees C ranged from 24.6 to 114 mug/l of natural pyrethrins and from 0.110 to 1,140 mug/l of pyrethroids. Two pyrethroids, RU-11679 and SBP-1382 (R), were over 10 times more toxic than pyrethrum extract in the flow-through tests. Coldwater species of fish were more sensitive than warmwater species to all the compunds. Temperature (12-22 degrees C) influences the toxicity of natural pyrethrin and the pyrethroids. The natural pyrethrin was more toxic to fish in pH 6.5 than in pH 9.5 water, but the toxicity of pyrethroids was not influenced in the pH range. The two most toxic pyrethroids, RU-11679 and SBP-1382, Were deactivated more rapidly in water solutions than natural pyrethrins, S-bioallethrin, dimethrin, and d-trans allethrin. | Toxicity of natural pyrethrins and five pyrethroids to fish. The toxicity of natural pyrethrins and five pyrethroids was determined with coho salmon (Oncorhynchus kisutch), steelhead trout (Salmo gairdneri), fathead minnow (Pimephales promelas), channel catfish (Icatlurus punctatus), bluegill (Lepomis macrochirus), and yellow perch (Perca flavescens). The 96-hour LC50's in static tests at 12 degrees C ranged from 24.6 to 114 mug/l of natural pyrethrins and from 0.110 to 1,140 mug/l of pyrethroids. Two pyrethroids, RU-11679 and SBP-1382 (R), were over 10 times more toxic than pyrethrum extract in the flow-through tests. Coldwater species of fish were more sensitive than warmwater species to all the compunds. Temperature (12-22 degrees C) influences the toxicity of natural pyrethrin and the pyrethroids. The natural pyrethrin was more toxic to fish in pH 6.5 than in pH 9.5 water, but the toxicity of pyrethroids was not influenced in the pH range. The two most toxic pyrethroids, RU-11679 and SBP-1382, Were deactivated more rapidly in water solutions than natural pyrethrins, S-bioallethrin, dimethrin, and d-trans allethrin. | [
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PMID:5060 | Acute toxicity of selenium dioxide to freshwater fishes. | Acute toxicity tests of selenium dioxide were conducted for 96 to 336 hr in intermittent-flow bioassay systems using six species of freshwater fish. The decreasing order of species sensitivity was: fathead minnow, flagfish, brook trout, channel catfish, goldfish, and bluegil. Curves relating median lethal concentration to exposure time for each species exposed for more than 168 hr were sigmoid in shape and were characterized by a change in slope indicating a more rapid mortality rate after 96 to 168 hr toxicant exposure. The 96-hr LC50 estimates ranged from 2.9 mg/L SeO2 for fathead minnow fry to 40.0 mg/L for bluegill juveniles. Effects of brief toxicant exposure (24 hr) on fathead minnow and flagfish juveniles included limited delayed mortality and no effects on growth over a 28-day period. | Acute toxicity of selenium dioxide to freshwater fishes. Acute toxicity tests of selenium dioxide were conducted for 96 to 336 hr in intermittent-flow bioassay systems using six species of freshwater fish. The decreasing order of species sensitivity was: fathead minnow, flagfish, brook trout, channel catfish, goldfish, and bluegil. Curves relating median lethal concentration to exposure time for each species exposed for more than 168 hr were sigmoid in shape and were characterized by a change in slope indicating a more rapid mortality rate after 96 to 168 hr toxicant exposure. The 96-hr LC50 estimates ranged from 2.9 mg/L SeO2 for fathead minnow fry to 40.0 mg/L for bluegill juveniles. Effects of brief toxicant exposure (24 hr) on fathead minnow and flagfish juveniles included limited delayed mortality and no effects on growth over a 28-day period. | [
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PMID:5061 | Effect of alpha and beta adrenergic blockade on epinephrine induced pulmonary insufficiency. | Recent studies demonstrated that epinephrine causes significant pulmonary A-V shunting. This study reports the effect of alpha and beta adrenergic blockade on this shunting. Sixty-three anesthetized mongrel dogs were ventilated with a mechanical respirator. Measurements of (1) the pulmonary shunt, (2) cardiac output, (3) mean pulmonary artery, pulmonary capillary wedge and systemic pressures, and (4) pulmonary and systemic vascular resistances were obtained at 5, 15 and 30 minute intervals during the first hour and hourly for 5 hours. Fifteen dogs received no treatment. All others received epinephrine hydrochloride, 2 mug/kg/min for 5 hours. Ten received epinephrine only. Ten were pretreated with propranolol hydrochloride, 250 mug/kg, 12 with phenoxybenzamine, 1 mg/kg, and 16 with phenoxybenzamine and propranolol. Propranolol significantly decreased the epinephrine induced pulmonary shunt at all times and was the most effective drug. Phenoxybenzamine decreased the early shunting, but less than propranolol, and did not decrease the late shunting. Blockade with propranolol and phenoxybenzamine was less effective than propranolol alone. Based on the observed hemodynamic changes it was suggested that beta blockade is effective in reducing epinephrine induced pulmonary insufficiency by favorably altering the flow and distribution of pulmonary blood flow which in turn decreases epinephrine induced ventilation-perfusion inequalities and capillary hypertension both of which result in shunting. Conversely phenoxybenzamine has an unfavorable effect on the pulmonary flow. These studies support previous work in animals and man which showed that beta adrenergic stimulation is important in the pathogenesis of pulmonary insufficiency. Because the amounts of epinephrine used produce blood levels observed in critical illness, these studies add support to a relationship between the increased catecholamine stimulation of critical illness and the associated and often unexplained pulmonary insufficiency. | Effect of alpha and beta adrenergic blockade on epinephrine induced pulmonary insufficiency. Recent studies demonstrated that epinephrine causes significant pulmonary A-V shunting. This study reports the effect of alpha and beta adrenergic blockade on this shunting. Sixty-three anesthetized mongrel dogs were ventilated with a mechanical respirator. Measurements of (1) the pulmonary shunt, (2) cardiac output, (3) mean pulmonary artery, pulmonary capillary wedge and systemic pressures, and (4) pulmonary and systemic vascular resistances were obtained at 5, 15 and 30 minute intervals during the first hour and hourly for 5 hours. Fifteen dogs received no treatment. All others received epinephrine hydrochloride, 2 mug/kg/min for 5 hours. Ten received epinephrine only. Ten were pretreated with propranolol hydrochloride, 250 mug/kg, 12 with phenoxybenzamine, 1 mg/kg, and 16 with phenoxybenzamine and propranolol. Propranolol significantly decreased the epinephrine induced pulmonary shunt at all times and was the most effective drug. Phenoxybenzamine decreased the early shunting, but less than propranolol, and did not decrease the late shunting. Blockade with propranolol and phenoxybenzamine was less effective than propranolol alone. Based on the observed hemodynamic changes it was suggested that beta blockade is effective in reducing epinephrine induced pulmonary insufficiency by favorably altering the flow and distribution of pulmonary blood flow which in turn decreases epinephrine induced ventilation-perfusion inequalities and capillary hypertension both of which result in shunting. Conversely phenoxybenzamine has an unfavorable effect on the pulmonary flow. These studies support previous work in animals and man which showed that beta adrenergic stimulation is important in the pathogenesis of pulmonary insufficiency. Because the amounts of epinephrine used produce blood levels observed in critical illness, these studies add support to a relationship between the increased catecholamine stimulation of critical illness and the associated and often unexplained pulmonary insufficiency. | [
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PMID:5062 | Revascularization of the heart through the coronary veins. | Fifty-six dogs were used in a study to evaluate perfusion of the left anterior descending vein by the internal mammary artery in hearts with normal coronary arteries and those with ligated desending coronary arteries. Perfusion of the myocardium with arterial blood through the cardiac veins offers minimal immediate protection from infarction, as evidenced by light and electron microscopy studies. This protection is of short duration due to intimal fibrosis and luminal stenosis or obstruction of the perfused veins. Nineteen animals in which the coronary vein was perfused and the corresponding coronary artery was not ligated died within sixty hours from the time of operation. Pathological examination revealed patent grafts in all the animals. There was marked congestion of the myocardium with petechial hemorrhages over the surface of the heart. No evidence of myocardial infarction was found. | Revascularization of the heart through the coronary veins. Fifty-six dogs were used in a study to evaluate perfusion of the left anterior descending vein by the internal mammary artery in hearts with normal coronary arteries and those with ligated desending coronary arteries. Perfusion of the myocardium with arterial blood through the cardiac veins offers minimal immediate protection from infarction, as evidenced by light and electron microscopy studies. This protection is of short duration due to intimal fibrosis and luminal stenosis or obstruction of the perfused veins. Nineteen animals in which the coronary vein was perfused and the corresponding coronary artery was not ligated died within sixty hours from the time of operation. Pathological examination revealed patent grafts in all the animals. There was marked congestion of the myocardium with petechial hemorrhages over the surface of the heart. No evidence of myocardial infarction was found. | [
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PMID:5063 | Dirofilaria immitis (dog heartworm) as a pulmonary lesion in humans. | Dirofilaria immitis, the dog heartworm, has been identified in the pulmonary granulomas of 5 patients from the greater Charleston area; this is the largest series of such cases from one medical center. The patients had no pulmonary symptoms. On roentgenogram the lesions were all about 2 cm in size, of uniform light opacity, and located near the pleural surface. Thoractomy was performed in each instance because of the possiblity of carcinoma. The association of granuloma formation, pulmonary infarct, and eosinophilic infiltration led to the suspicion of dirofilaria, which was confirmed in each case. | Dirofilaria immitis (dog heartworm) as a pulmonary lesion in humans. Dirofilaria immitis, the dog heartworm, has been identified in the pulmonary granulomas of 5 patients from the greater Charleston area; this is the largest series of such cases from one medical center. The patients had no pulmonary symptoms. On roentgenogram the lesions were all about 2 cm in size, of uniform light opacity, and located near the pleural surface. Thoractomy was performed in each instance because of the possiblity of carcinoma. The association of granuloma formation, pulmonary infarct, and eosinophilic infiltration led to the suspicion of dirofilaria, which was confirmed in each case. | [
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PMID:5064 | Benorylate interaction with indomethacin and phenylbutazone. | The simlutaneous oral administration of benorylate (4-(acetamido) phenyl 2-acetoxybenzoate) with either indomethacin or phenylbutazone to rats suffering from Freund's adjuvant-induced arthritis leads to an anti-inflammatory effect which is significantly greater than the effect of the same drugs administered alone. Such an additive anti-inflammatory effect is not apparent when the metabolites of benorylate (paracetamol, acetylsalicylic acid) are administered with indomethacin or phenylbutazone. Paracetamol does not increase the anti-inflammatory effect of indomethacin or phenylbutazone and acetylsalicylic acid clearly antagonizes it. The molecule of benorylate itsel is therefore responsible for the additive anti-inflammatory effect. However, if antipyretic activity (yeast-induced hyperthermia) is examined instead of anti-inflammatory activity, the simultaneous oral administration of the different drugs always produces an additive effect. It is concluded that the antagonism between indomethacin or phenylbutazone and non-steroidal anti-inflammatory drugs other than benorylate is present at some receptors but not all. The clinical implications of the results are discussed. | Benorylate interaction with indomethacin and phenylbutazone. The simlutaneous oral administration of benorylate (4-(acetamido) phenyl 2-acetoxybenzoate) with either indomethacin or phenylbutazone to rats suffering from Freund's adjuvant-induced arthritis leads to an anti-inflammatory effect which is significantly greater than the effect of the same drugs administered alone. Such an additive anti-inflammatory effect is not apparent when the metabolites of benorylate (paracetamol, acetylsalicylic acid) are administered with indomethacin or phenylbutazone. Paracetamol does not increase the anti-inflammatory effect of indomethacin or phenylbutazone and acetylsalicylic acid clearly antagonizes it. The molecule of benorylate itsel is therefore responsible for the additive anti-inflammatory effect. However, if antipyretic activity (yeast-induced hyperthermia) is examined instead of anti-inflammatory activity, the simultaneous oral administration of the different drugs always produces an additive effect. It is concluded that the antagonism between indomethacin or phenylbutazone and non-steroidal anti-inflammatory drugs other than benorylate is present at some receptors but not all. The clinical implications of the results are discussed. | [
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PMID:5066 | A controlled trial of amantadine in drug-induced extrapyramidal disorders. | Presently marketed antiparkinsonism drugs are potent anticholinergic agents that, while effective in treating extrapyramidal symptoms (EPS), also are productive of or can exacerbate a number of side effects associated with psychotropic drugs. Some of these include gastrointestinal disturbances, visual difficulties, and tardive dyskinesia. A double-blind study was carried out to assess the efficacy (and adverse effects) of amantadine hydrochloride--an agent without appreciable anticholinergic activity--for the treatment of drug-induced EPS. Amantadine was found to be comparable in effect to benztropine mesylate, but with fewer side effects. The potential role of amantadine may be in the treatment of patients with drug-induced EPS for whom medication with anticholinergic properties is contraindicated. | A controlled trial of amantadine in drug-induced extrapyramidal disorders. Presently marketed antiparkinsonism drugs are potent anticholinergic agents that, while effective in treating extrapyramidal symptoms (EPS), also are productive of or can exacerbate a number of side effects associated with psychotropic drugs. Some of these include gastrointestinal disturbances, visual difficulties, and tardive dyskinesia. A double-blind study was carried out to assess the efficacy (and adverse effects) of amantadine hydrochloride--an agent without appreciable anticholinergic activity--for the treatment of drug-induced EPS. Amantadine was found to be comparable in effect to benztropine mesylate, but with fewer side effects. The potential role of amantadine may be in the treatment of patients with drug-induced EPS for whom medication with anticholinergic properties is contraindicated. | [
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PMID:5067 | Metabolism and ultrastructure in ovaries of alloxan-diabetic juvenile rats. | Tests were carried out on the influence of alloxan-induced diabetes mellitus on the metabolism and the ultrastructure of ovaries of juvenile rats. The diabetes mellitus caused the following changes in the metabolism: reduction in the concentration of ATP and NADPH, increase in the lactate/pyruvate quotient to above 40, reduction in the ATP/ADP quotient to below 1, reduction in the level of activity of the hydrogen-conveying enzymes G-6-P-dehydrogenase, isocitrate dehydrogenase and malate dehydrogenase, increase in the level of activity of the alkaline phosphatase, reduction of the protein content. Ultrastructure: almost complete disappearance of the rough endoplasmic reticulum, shrinkage of the mitochondria, reduction of the cristae and condensation of the matrix. The smooth endoplasmic reticulum remains unchanged, the extent of the Golgi-complex is reduced. Easy removal of the lipid deposits. | Metabolism and ultrastructure in ovaries of alloxan-diabetic juvenile rats. Tests were carried out on the influence of alloxan-induced diabetes mellitus on the metabolism and the ultrastructure of ovaries of juvenile rats. The diabetes mellitus caused the following changes in the metabolism: reduction in the concentration of ATP and NADPH, increase in the lactate/pyruvate quotient to above 40, reduction in the ATP/ADP quotient to below 1, reduction in the level of activity of the hydrogen-conveying enzymes G-6-P-dehydrogenase, isocitrate dehydrogenase and malate dehydrogenase, increase in the level of activity of the alkaline phosphatase, reduction of the protein content. Ultrastructure: almost complete disappearance of the rough endoplasmic reticulum, shrinkage of the mitochondria, reduction of the cristae and condensation of the matrix. The smooth endoplasmic reticulum remains unchanged, the extent of the Golgi-complex is reduced. Easy removal of the lipid deposits. | [
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PMID:5068 | Human tear pH. Diurnal variations. | Using a closed chamber microelectrode system, the tear pH levels of sixteen subjects were monitored throughout the waking extent of five days. In addition to the absolute mean pH differences found among subjects, diurnal patterns of pH change could be identified for the majority. The amplitudes and periods of these cycloid patterns, however, were distinctive to each individual. Also, tear pH levels following periods of prolonged eye closure were found to be notably more acid than those associated with the waking hours. | Human tear pH. Diurnal variations. Using a closed chamber microelectrode system, the tear pH levels of sixteen subjects were monitored throughout the waking extent of five days. In addition to the absolute mean pH differences found among subjects, diurnal patterns of pH change could be identified for the majority. The amplitudes and periods of these cycloid patterns, however, were distinctive to each individual. Also, tear pH levels following periods of prolonged eye closure were found to be notably more acid than those associated with the waking hours. | [
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PMID:5069 | Reactivity and ionization constants of the lysine residues in apovitellenin i of emu egg yolk low-density lipoprotein by competitive labelling. | Competitive labelling with[14C]acetic anhydride over a range of pH values has been used to explore the surface topography of the apovitellenin I moiety in emu egg yolk low-density lipoprotein. The reaction of the lysine xi-amino groups with acetic anhydride has been related to pH in a set of titration curves; from these, the reactivities relative to alanine and the ionization constants of all but the amino terminal lysines have been determined. All lysines have near normal pKa values around 10, and lower than normal reactivities (except the amino terminal lysine). At pH values above 10, the titration curves show breaks where the epsilon-amino groups become much more reactive, except for lysine 71 which in this regard behaves like a normally ionizing lysine in not showing a discontinuity. Most of the basic residues in this apoprotein may occur clustered at the surface of the molecule. This accounts best for the observed low reactivities and pKa values. The amino terminal lysine residue is presumably completely exposed to the aqueous environment. | Reactivity and ionization constants of the lysine residues in apovitellenin i of emu egg yolk low-density lipoprotein by competitive labelling. Competitive labelling with[14C]acetic anhydride over a range of pH values has been used to explore the surface topography of the apovitellenin I moiety in emu egg yolk low-density lipoprotein. The reaction of the lysine xi-amino groups with acetic anhydride has been related to pH in a set of titration curves; from these, the reactivities relative to alanine and the ionization constants of all but the amino terminal lysines have been determined. All lysines have near normal pKa values around 10, and lower than normal reactivities (except the amino terminal lysine). At pH values above 10, the titration curves show breaks where the epsilon-amino groups become much more reactive, except for lysine 71 which in this regard behaves like a normally ionizing lysine in not showing a discontinuity. Most of the basic residues in this apoprotein may occur clustered at the surface of the molecule. This accounts best for the observed low reactivities and pKa values. The amino terminal lysine residue is presumably completely exposed to the aqueous environment. | [
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PMID:5070 | Properties and specificity of a second metal chelator-sensitive proteinase in the keratinolytic larvae of the webbing clothes moth. | The properties of a second metal chelator-sensitive proteinase (metalloproteinase 2) from the larvae of the webbing clothes moth, Tineola bisselliella, have been studied. The pH optimum for casein digestion was 9-4 and the enzyme showed high stability between pH 8 and 11, but very poor stability at acid pH. The proteinase was inhibited by EDTA, but not by an EDTA-calcium complex. EDTA inhibition could be reversed by addition of a slight excess of calcium or zinc ions. The cleavage specificity of metalloproteinase 2 against the A and B chains of S-carboxymethyl insulin was almost identical to that found previously for metalloproteinase 1. | Properties and specificity of a second metal chelator-sensitive proteinase in the keratinolytic larvae of the webbing clothes moth. The properties of a second metal chelator-sensitive proteinase (metalloproteinase 2) from the larvae of the webbing clothes moth, Tineola bisselliella, have been studied. The pH optimum for casein digestion was 9-4 and the enzyme showed high stability between pH 8 and 11, but very poor stability at acid pH. The proteinase was inhibited by EDTA, but not by an EDTA-calcium complex. EDTA inhibition could be reversed by addition of a slight excess of calcium or zinc ions. The cleavage specificity of metalloproteinase 2 against the A and B chains of S-carboxymethyl insulin was almost identical to that found previously for metalloproteinase 1. | [
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PMID:5071 | Aminopeptidases in webbing clothes moth larvae. properties and specificities of enzymes of highest electrophoretic mobility. | The group of aminopeptidase bands from Tineola bisselliella larvae with highest electrophoretic mobility in polyacrylamide gels were purified further and partially separated by ion exchange chromatography. Three aminopeptidase bands were present in this material and were very similar with respect to their pH optima (7-7), their molecular weight of 94,000, their responses to metal ions and enzyme inhibitors and in their substrate specificity requirements. Kinetic constants were obtained for the hydrolysis of 17 different alpha-aminoacyl-beta-naphthylamides by these aminopeptidases, the most favoured substrates being the derivatives of alanine, methionine, proline, leucine, glycine, glutamic acid, lysine and arginine. The enzymes also hydrolyse amino acid amides, dipeptides, dipeptide amides, tripeptides and oligopeptides at the N-terminal end. These enzymes differ from the other aminopeptides in T. bisselliella in being able to hydrolyse bonds involving proline. | Aminopeptidases in webbing clothes moth larvae. properties and specificities of enzymes of highest electrophoretic mobility. The group of aminopeptidase bands from Tineola bisselliella larvae with highest electrophoretic mobility in polyacrylamide gels were purified further and partially separated by ion exchange chromatography. Three aminopeptidase bands were present in this material and were very similar with respect to their pH optima (7-7), their molecular weight of 94,000, their responses to metal ions and enzyme inhibitors and in their substrate specificity requirements. Kinetic constants were obtained for the hydrolysis of 17 different alpha-aminoacyl-beta-naphthylamides by these aminopeptidases, the most favoured substrates being the derivatives of alanine, methionine, proline, leucine, glycine, glutamic acid, lysine and arginine. The enzymes also hydrolyse amino acid amides, dipeptides, dipeptide amides, tripeptides and oligopeptides at the N-terminal end. These enzymes differ from the other aminopeptides in T. bisselliella in being able to hydrolyse bonds involving proline. | [
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PMID:5100 | Anti-leukaemia activity as a bystander effect of graft-versus-host reactions. | The production of graft-versus-host (GVH) reactions in (PVGc X Wistar) F1 hybrids by the transfer of PVGc spleen cells resulted in significant resistance of these recipients to a subsequent challenge with the PVGc leukaemia. Protection was markedly dependent on dose and timing of allogeneic cell transfer and was abrogated by irradiation of the cells prior to transfer. GVH activity was shown to be a prerequisite for induction of the protective effect but was equally effective when produced by the transfer of Wistar spleen cells in place of PVGc cells. These points, plus the fact that invitro investigations of possible immune mechanisms failed to demonstrate cytotoxic immunity in treated rats, suggested a nonspecific "bystander" effect as the mechanism of protection. The implications of such a mechanism are discussed. | Anti-leukaemia activity as a bystander effect of graft-versus-host reactions. The production of graft-versus-host (GVH) reactions in (PVGc X Wistar) F1 hybrids by the transfer of PVGc spleen cells resulted in significant resistance of these recipients to a subsequent challenge with the PVGc leukaemia. Protection was markedly dependent on dose and timing of allogeneic cell transfer and was abrogated by irradiation of the cells prior to transfer. GVH activity was shown to be a prerequisite for induction of the protective effect but was equally effective when produced by the transfer of Wistar spleen cells in place of PVGc cells. These points, plus the fact that invitro investigations of possible immune mechanisms failed to demonstrate cytotoxic immunity in treated rats, suggested a nonspecific "bystander" effect as the mechanism of protection. The implications of such a mechanism are discussed. | [
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PMID:5101 | The effect of aflatoxins on the incorporation of RNA and protein precursors by isolated hepatocytes. | Hepatocytes prepared by a simplified enzymatic technique were active in the incorporation of RNA and protein precursors into acid-insoluble material. The incorporation of RNA precursors was very markedly inhibited by low levels of aflatoxin B1 and G1 but not by aflatoxins B2 and G2. The activity of mixed function oxidases (MFO), the drug-metabolizing system of the endoplasmic reticulum, could be suppressed in these cells by SKF525A or stimulated by NADPH. SKF525A caused a reduction in the inhibition by aflatoxin B1 of the incorporation of RNA precursor into macromolecules. This finding suggests that a metabolite of aflatoxin B1 is the actual inhibitor of RNA synthesis in the cells. Measurement of lactate dehydrogenase activity showed these cells to be leaky on incubation at 37 degrees C and thus not suitable for studies of protein secretion. | The effect of aflatoxins on the incorporation of RNA and protein precursors by isolated hepatocytes. Hepatocytes prepared by a simplified enzymatic technique were active in the incorporation of RNA and protein precursors into acid-insoluble material. The incorporation of RNA precursors was very markedly inhibited by low levels of aflatoxin B1 and G1 but not by aflatoxins B2 and G2. The activity of mixed function oxidases (MFO), the drug-metabolizing system of the endoplasmic reticulum, could be suppressed in these cells by SKF525A or stimulated by NADPH. SKF525A caused a reduction in the inhibition by aflatoxin B1 of the incorporation of RNA precursor into macromolecules. This finding suggests that a metabolite of aflatoxin B1 is the actual inhibitor of RNA synthesis in the cells. Measurement of lactate dehydrogenase activity showed these cells to be leaky on incubation at 37 degrees C and thus not suitable for studies of protein secretion. | [
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PMID:5102 | Passive serum sickness in the mouse: the role of vasoactive amines in glomerular deposition of immune complexes. | This paper reports a study of the importance of vasoactive amines in glomerular localization of passively administered immune complexes in the mouse. Two strains of mice were investigated, one sensitive and the other relatively resistant to the anaphylactogenic effect of intravenously administered immune complexes. The effect on glomerular deposition immune complexes in animals of both strains treated with either vasoactive amine depletors or antagonists leads to the conclusion that in this experimental system vasoactive amines do not play a major part in the glomerular localization of immune complexes. | Passive serum sickness in the mouse: the role of vasoactive amines in glomerular deposition of immune complexes. This paper reports a study of the importance of vasoactive amines in glomerular localization of passively administered immune complexes in the mouse. Two strains of mice were investigated, one sensitive and the other relatively resistant to the anaphylactogenic effect of intravenously administered immune complexes. The effect on glomerular deposition immune complexes in animals of both strains treated with either vasoactive amine depletors or antagonists leads to the conclusion that in this experimental system vasoactive amines do not play a major part in the glomerular localization of immune complexes. | [
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PMID:5104 | Intensive care of the fetus in breech labour. | A review of 186 cases of breech presentation with a corrected perinatal mortality rate of 0-54 per cent is presented. Details of paediatric follow-up are given. Careful selection of patients for vaginal delivery and the liberal use of Caesarean section are advocated. The importance of asphyxia as the main danger of breech delivery is emphasized and the use of fetal blood sampling as a practicable method of detecting early asphyxia is discussed. | Intensive care of the fetus in breech labour. A review of 186 cases of breech presentation with a corrected perinatal mortality rate of 0-54 per cent is presented. Details of paediatric follow-up are given. Careful selection of patients for vaginal delivery and the liberal use of Caesarean section are advocated. The importance of asphyxia as the main danger of breech delivery is emphasized and the use of fetal blood sampling as a practicable method of detecting early asphyxia is discussed. | [
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PMID:5105 | The effects of grass and concentrate diets on the specific activities of some enzymes of hepatic carbohydrate metabolism in sheep. | Feeding sheep a concentrate diet compared with grass diets increased the hepatic specific activities of the three glycolytic enzymes studied, and that of glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and reduced the specific activity of D-fructose-I, 6-diphosphate I-phosphohydrolase (EC 3.1.3.11). The specific activities of phosphogluconate dehydrogenase (EC 1.1.1.43) and malate dehydrogenase (decarboxylating) (NADP) (EC 1.1.1.40) were unaffected by diet. | The effects of grass and concentrate diets on the specific activities of some enzymes of hepatic carbohydrate metabolism in sheep. Feeding sheep a concentrate diet compared with grass diets increased the hepatic specific activities of the three glycolytic enzymes studied, and that of glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and reduced the specific activity of D-fructose-I, 6-diphosphate I-phosphohydrolase (EC 3.1.3.11). The specific activities of phosphogluconate dehydrogenase (EC 1.1.1.43) and malate dehydrogenase (decarboxylating) (NADP) (EC 1.1.1.40) were unaffected by diet. | [
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PMID:5106 | Light-induced glutamate transport in Halobacterium halobium envelope vesicles. II. Evidence that the driving force is a light-dependent sodium gradient. | Illumination of cell envelope vesicles from H. halobium causes the development of protonmotive force and energizes the uphill transport of glutamate. Although the uncoupler, p-trifluoromethoxycarbonyl cyanide phenylhydrazone (FCCP), and the membrane-permeant cation, triphenylmethylphosphonium (TPMP+), are inhibitory to the effect of light, the time course and kinetics of the production of the energized state for transport, and its rate of decay after illumination, are inconsistent with the idea that glutamate accumulation is driven directly by the protonmotive force. Similarities between the light-induced transport and the Na+-gradient-induced transport of glutamate in these vesicles suggest that the energized state for the amino acid uptake in both cases consists of a transmembrane Na+ gradient (Na+out/Na+in greater than 1). Rapid efflux of 22Na from the envelope vesicles is induced by illumination. FCCP and TPMP+ inhibit the light-induced efflux of Na+ but accelerate the post-illumination relaxation of the Na+ gradient created, suggesting electrogenic antiport of Na+ with another cation, or electrogenic symport with an anion. The light-induced protonmotive force in the H. halobium cell envelope vesicles is thus coupled to Na+ efflux and thereby indirectly to glutamate uptake as well. | Light-induced glutamate transport in Halobacterium halobium envelope vesicles. II. Evidence that the driving force is a light-dependent sodium gradient. Illumination of cell envelope vesicles from H. halobium causes the development of protonmotive force and energizes the uphill transport of glutamate. Although the uncoupler, p-trifluoromethoxycarbonyl cyanide phenylhydrazone (FCCP), and the membrane-permeant cation, triphenylmethylphosphonium (TPMP+), are inhibitory to the effect of light, the time course and kinetics of the production of the energized state for transport, and its rate of decay after illumination, are inconsistent with the idea that glutamate accumulation is driven directly by the protonmotive force. Similarities between the light-induced transport and the Na+-gradient-induced transport of glutamate in these vesicles suggest that the energized state for the amino acid uptake in both cases consists of a transmembrane Na+ gradient (Na+out/Na+in greater than 1). Rapid efflux of 22Na from the envelope vesicles is induced by illumination. FCCP and TPMP+ inhibit the light-induced efflux of Na+ but accelerate the post-illumination relaxation of the Na+ gradient created, suggesting electrogenic antiport of Na+ with another cation, or electrogenic symport with an anion. The light-induced protonmotive force in the H. halobium cell envelope vesicles is thus coupled to Na+ efflux and thereby indirectly to glutamate uptake as well. | [
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PMID:5107 | Physical studies of the nonhistone chromosomal proteins HMG-U and HMG-2. | The nonhistone chromosomal proteins, HMG-1 and HMG-2, have a folded conformation, with a high alpha-helical content, over a wide pH range. At high and low pH values, the molecules unfold. Both molecules contain cysteine and tryptophan. The tryptophans appear to be buried in the folded form. HMG-1 shows aggregation at pH 5.7, as does HMG-2 at pH 9.0. The folded form is insensitive to high concentrations of salt, suggesting that charge-charge interaction plays no role in stabilizing the tertiary structure. | Physical studies of the nonhistone chromosomal proteins HMG-U and HMG-2. The nonhistone chromosomal proteins, HMG-1 and HMG-2, have a folded conformation, with a high alpha-helical content, over a wide pH range. At high and low pH values, the molecules unfold. Both molecules contain cysteine and tryptophan. The tryptophans appear to be buried in the folded form. HMG-1 shows aggregation at pH 5.7, as does HMG-2 at pH 9.0. The folded form is insensitive to high concentrations of salt, suggesting that charge-charge interaction plays no role in stabilizing the tertiary structure. | [
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PMID:5108 | Synthesis and properties of carbonylbis(methionyl)insulin, a proinsulin analogue which is convertible to insulin by cyanogen bromide cleavage. | The preparation and use of carbonylbis (L-methionine p-nitrophenyl ester) as a reversible cross-linking reagent for insulin are described. The reaction of 1 equiv of reagent with zinc insulin in dimethylformamide in the presence of triethylamine yields as one of the products NalphaA1, NepsilonB29-carbonylbis(methionyl)insulin, (CBM-insulin). The CBM-insulin was characterized by end group analysis and by the products formed on tryptic and chymotryptic cleavage. It possessed 91% of the immunological and 6.5% of the hormonal activity of insulin. Treatment of CBM-insulin with cyanogen bromide (CNBr) in 70% formic acid for 1 h resulted in nearly complete removal of the methionine bridge to yield insulin. A small amount of a side product was removed on DEAE-cellulose at pH 7.2 to give an overall recovery of insulin of 70-80%. Oxidative sulfitolyses of CBM-insulin gave the hexa(S-sulfonate) which was reduced with dithiothreitol to yield reduced CBM-insulin. The latter compound, containing 6 sulfhydryls, exhibited a pH-dependent circular dichroic spectrum. The form at pH 10 exhibited a spectrum typical of random coil which was converted to a form at pH 7.8 which was characterized by a negative extremum at 213 nm. The change in the spectrum at 213 nm with pH was characterized by an apparent pKa of 8.5. Studies on the reoxidation of reduced CBM-insulin were performed at pH values between 7.8 and 10 and at protein concentrations of 0.01-1 mg/ml. The best yields (ca. 85%) of the correctly paired disulfide bonds were obtained in reoxidations at pH 9.5-10 at protein concentration of 0.01-0.1 mg/ml. CBM-insulin, which had been isolated from reoxidation at high pH of the reduced CBM-insulin, was cleaved by CNBr to yield a fully active insulin in an overall yield of 60% from the reduced CBM-insulin. | Synthesis and properties of carbonylbis(methionyl)insulin, a proinsulin analogue which is convertible to insulin by cyanogen bromide cleavage. The preparation and use of carbonylbis (L-methionine p-nitrophenyl ester) as a reversible cross-linking reagent for insulin are described. The reaction of 1 equiv of reagent with zinc insulin in dimethylformamide in the presence of triethylamine yields as one of the products NalphaA1, NepsilonB29-carbonylbis(methionyl)insulin, (CBM-insulin). The CBM-insulin was characterized by end group analysis and by the products formed on tryptic and chymotryptic cleavage. It possessed 91% of the immunological and 6.5% of the hormonal activity of insulin. Treatment of CBM-insulin with cyanogen bromide (CNBr) in 70% formic acid for 1 h resulted in nearly complete removal of the methionine bridge to yield insulin. A small amount of a side product was removed on DEAE-cellulose at pH 7.2 to give an overall recovery of insulin of 70-80%. Oxidative sulfitolyses of CBM-insulin gave the hexa(S-sulfonate) which was reduced with dithiothreitol to yield reduced CBM-insulin. The latter compound, containing 6 sulfhydryls, exhibited a pH-dependent circular dichroic spectrum. The form at pH 10 exhibited a spectrum typical of random coil which was converted to a form at pH 7.8 which was characterized by a negative extremum at 213 nm. The change in the spectrum at 213 nm with pH was characterized by an apparent pKa of 8.5. Studies on the reoxidation of reduced CBM-insulin were performed at pH values between 7.8 and 10 and at protein concentrations of 0.01-1 mg/ml. The best yields (ca. 85%) of the correctly paired disulfide bonds were obtained in reoxidations at pH 9.5-10 at protein concentration of 0.01-0.1 mg/ml. CBM-insulin, which had been isolated from reoxidation at high pH of the reduced CBM-insulin, was cleaved by CNBr to yield a fully active insulin in an overall yield of 60% from the reduced CBM-insulin. | [
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PMID:5109 | DNA-dependent RNA polymerase from the thermophilic bacterium Caldariella acidophila. Purification and basic properties of the enzyme. | A DNA-dependent RNA polymerase has been isolated from Caldariella acidophila, a thermophilic bacterium living in acidic hot springs at temperatures ranging from 63 to 89 degrees C. The enzyme was purified 180-fold and is composed of five different subunits having the following molecular weights: a = 127000, b = 120000, c = 72000, d = 65000, and e = 38000. The enzyme is activated by Mn2+ and Mg2+ and exhibits optimal activity in the presence of 0.5 mM Mn2+. The activity depends on ionic strength, with a maximum at 0.25 M KCl, and exhibits a pH optimum at 7.8 in the presence of Tris-HCl buffer. The enzyme shows a high degree of thermophilicity, its temperature optimum being 80 degrees C in the in vitro assay. The thermophilicity of C. acidophila RNA polymerase allows studies on enzyme-template interactions to be performed in a temperature range where many templates are close to their Tm. | DNA-dependent RNA polymerase from the thermophilic bacterium Caldariella acidophila. Purification and basic properties of the enzyme. A DNA-dependent RNA polymerase has been isolated from Caldariella acidophila, a thermophilic bacterium living in acidic hot springs at temperatures ranging from 63 to 89 degrees C. The enzyme was purified 180-fold and is composed of five different subunits having the following molecular weights: a = 127000, b = 120000, c = 72000, d = 65000, and e = 38000. The enzyme is activated by Mn2+ and Mg2+ and exhibits optimal activity in the presence of 0.5 mM Mn2+. The activity depends on ionic strength, with a maximum at 0.25 M KCl, and exhibits a pH optimum at 7.8 in the presence of Tris-HCl buffer. The enzyme shows a high degree of thermophilicity, its temperature optimum being 80 degrees C in the in vitro assay. The thermophilicity of C. acidophila RNA polymerase allows studies on enzyme-template interactions to be performed in a temperature range where many templates are close to their Tm. | [
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PMID:5110 | Induction of stable protein-deoxyribonucleic acid adducts in Chinese hamster cell chromatin by ultraviolet light. | Ultraviolet (uv)-light-mediated formation of protein-DNA adducts in Chinese hamster cell chromatin was investigated in an attempt to compare chromatin alterations induced in vitro with those observed in vivo. Three independent methods of analysis indicated stable protein-DNA associations: (1) a membrane filter assay which retained DNA on the filter in the presence of high salt-detergent; (2) a Sepharose 4B column assay in which protein eluted cincident with DNA; and (3) a CsCl density gradient equilibrium assay which showed both protein and DNA banding at densities other than their respective native densities. Treatment of the irradiated chromatin with DNase provided further evidence that protein-DNA and not protein-protein adducts were being observed in the column assay. There is a fluence-dependent response of protein-DNA adduct formation when the chromatin is irradiated at low ionic strength and is linear for protein over the range studied. When the chromatin is exposed to differing conditions of pH, ionic strength, or divalent metal ion concentration, the quantity of adduct formed upon uv irradiation varies. Susceptibility to adduct formation can be partially explained in terms of the condensation state of the chromatin and other factors such as rearrangement, denaturation, and dissociation of the chromatin components. Besides providing information on the biological significance of these types of uv-induced lesions, this technique may be useful as a probe of chromatin structure. | Induction of stable protein-deoxyribonucleic acid adducts in Chinese hamster cell chromatin by ultraviolet light. Ultraviolet (uv)-light-mediated formation of protein-DNA adducts in Chinese hamster cell chromatin was investigated in an attempt to compare chromatin alterations induced in vitro with those observed in vivo. Three independent methods of analysis indicated stable protein-DNA associations: (1) a membrane filter assay which retained DNA on the filter in the presence of high salt-detergent; (2) a Sepharose 4B column assay in which protein eluted cincident with DNA; and (3) a CsCl density gradient equilibrium assay which showed both protein and DNA banding at densities other than their respective native densities. Treatment of the irradiated chromatin with DNase provided further evidence that protein-DNA and not protein-protein adducts were being observed in the column assay. There is a fluence-dependent response of protein-DNA adduct formation when the chromatin is irradiated at low ionic strength and is linear for protein over the range studied. When the chromatin is exposed to differing conditions of pH, ionic strength, or divalent metal ion concentration, the quantity of adduct formed upon uv irradiation varies. Susceptibility to adduct formation can be partially explained in terms of the condensation state of the chromatin and other factors such as rearrangement, denaturation, and dissociation of the chromatin components. Besides providing information on the biological significance of these types of uv-induced lesions, this technique may be useful as a probe of chromatin structure. | [
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PMID:5111 | D-Mannitol dehydrogenase from Absidia glauca. Purification, metabolic role, and subunit interactions. | When Absidia glauca was grown in minimal media with D-mannitol as the only source of carbon, an NAD+ specific D-mannitol dehydrogenase (EC 1.1.1.67) was induced. The crude extract also gave evidence of mannitol kinase, mannitol-1-phosphate dehydrogenase, phosphofructokinase, and L-iditol dehydrogenase activity. The heat labile purified preparation was judged enzymically homogeneous based on evidence derived from substrate specificity studies and activity staining, following disc gel electrophoresis. The enzymic monomer, with a weight of about 67000 daltons, slowly polymerizes when stored at -20 degrees C, giving a multiplicity of protein bands on electrophoresis distributed predominantly across a spectrum from dimer to pentamer, with enzymic activity resident predominantly in even multiples of the monomer. Depolymerization occurred rapidly (hours) when a frozen preparation was brought to and held between 4 and 20 degrees C. Aggregate fragmentation with sodium dodecyl sulfate showed a time-temperature dependence, terminating in a subunit component of 13000 daltons. pH optimum for polyol oxidation occurs at 9.6 (NaOH-glycine buffer) while ketose reduction proceeded most rapidly at pH 7.0-7.2 (phosphate buffer). A regulatory role is suggested for this enzyme based on dead-end inhibition by mannitol 1-phosphate, multiple enzyme forms, and its locus at the initiation site for mannitol utilization. The physiological relevance of low-temperature aggregation to regulatory control remains to be established. | D-Mannitol dehydrogenase from Absidia glauca. Purification, metabolic role, and subunit interactions. When Absidia glauca was grown in minimal media with D-mannitol as the only source of carbon, an NAD+ specific D-mannitol dehydrogenase (EC 1.1.1.67) was induced. The crude extract also gave evidence of mannitol kinase, mannitol-1-phosphate dehydrogenase, phosphofructokinase, and L-iditol dehydrogenase activity. The heat labile purified preparation was judged enzymically homogeneous based on evidence derived from substrate specificity studies and activity staining, following disc gel electrophoresis. The enzymic monomer, with a weight of about 67000 daltons, slowly polymerizes when stored at -20 degrees C, giving a multiplicity of protein bands on electrophoresis distributed predominantly across a spectrum from dimer to pentamer, with enzymic activity resident predominantly in even multiples of the monomer. Depolymerization occurred rapidly (hours) when a frozen preparation was brought to and held between 4 and 20 degrees C. Aggregate fragmentation with sodium dodecyl sulfate showed a time-temperature dependence, terminating in a subunit component of 13000 daltons. pH optimum for polyol oxidation occurs at 9.6 (NaOH-glycine buffer) while ketose reduction proceeded most rapidly at pH 7.0-7.2 (phosphate buffer). A regulatory role is suggested for this enzyme based on dead-end inhibition by mannitol 1-phosphate, multiple enzyme forms, and its locus at the initiation site for mannitol utilization. The physiological relevance of low-temperature aggregation to regulatory control remains to be established. | [
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PMID:5112 | Glutamine synthetase of Bacillus stearothermophilus. Regulation, site interactions, and functional information. | The action of various feedback modifiers on Bacillus stearothermophilus glutamine synthetase has been investigated by initial velocity kinetics, using the Mn2+-stimulated biosynthetic assay at 55 degrees C. The most potent inhibitors, used singly, are AMP, L-glutamine, and L-alanine. Other modifiers of significance include glycine, CTP, L-histidine, glucosamine 6-phosphate, and GDP. Marked synergism of action is observed for AMP in the presence of L-glutamine, L-histidine, ADP, or glucosamine 6-phosphate (glucosamine-6-P), and for CTP with ADP or GDP. Inhibition by saturating levels of many modifiers is either less than 100%, or is not overcome by elevated substrate levels, or both. This argues for modifier binding sites separate from substrate sites, notably in the cases of AMP, L-glutamine, glycine, L-alanine, glucosamine-6-P, and CTP. Glycine and L-alanine are Vmax inhibitors, whereas L-glutamine, glucosamine-6-P, GDP, and CTP alter the binding of L-glutamate. ADP and L-histidine apparently can compete directly with MnATP, but AMP alters Mn-ATP binding from a separate site. The action of several modifiers requires or is enhanced by bound substrates. Considerable antagonistic interaction is observed in experiments with modifier pairs, but the most potent inhibitors show synergistic or cumulative (independent) interactions. One may interpret antagonistic effects as due to (a) overlapping modifier domains, or (b) separate but antagonistically interacting sites. Either interpretation leads to a scheme for modifier-substrate and modifier-modifier site interactions in which the thermophilic enzyme must maintain and stabilize a great deal of complex functional information under extreme environmental conditions. | Glutamine synthetase of Bacillus stearothermophilus. Regulation, site interactions, and functional information. The action of various feedback modifiers on Bacillus stearothermophilus glutamine synthetase has been investigated by initial velocity kinetics, using the Mn2+-stimulated biosynthetic assay at 55 degrees C. The most potent inhibitors, used singly, are AMP, L-glutamine, and L-alanine. Other modifiers of significance include glycine, CTP, L-histidine, glucosamine 6-phosphate, and GDP. Marked synergism of action is observed for AMP in the presence of L-glutamine, L-histidine, ADP, or glucosamine 6-phosphate (glucosamine-6-P), and for CTP with ADP or GDP. Inhibition by saturating levels of many modifiers is either less than 100%, or is not overcome by elevated substrate levels, or both. This argues for modifier binding sites separate from substrate sites, notably in the cases of AMP, L-glutamine, glycine, L-alanine, glucosamine-6-P, and CTP. Glycine and L-alanine are Vmax inhibitors, whereas L-glutamine, glucosamine-6-P, GDP, and CTP alter the binding of L-glutamate. ADP and L-histidine apparently can compete directly with MnATP, but AMP alters Mn-ATP binding from a separate site. The action of several modifiers requires or is enhanced by bound substrates. Considerable antagonistic interaction is observed in experiments with modifier pairs, but the most potent inhibitors show synergistic or cumulative (independent) interactions. One may interpret antagonistic effects as due to (a) overlapping modifier domains, or (b) separate but antagonistically interacting sites. Either interpretation leads to a scheme for modifier-substrate and modifier-modifier site interactions in which the thermophilic enzyme must maintain and stabilize a great deal of complex functional information under extreme environmental conditions. | [
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PMID:5113 | Mechanistic studies of glutamine synthetase from Escherichia coli: kinetics of ADP and orthophosphate binding to the unadenylylated enzyme. | The kinetics of protein fluorescence change exhibited by ADP or orthophosphate addition to the Mg2+-or Mn2+-activated unadenylylated glutamine synthetase from Escherichia coli were studied. The kinetic patterns of these reactions are incompatible with a simple bimolecular binding process and a mechanism which required protein isomerization prior to substrate binding. They are consistent with a mechanism in which direct substrate binding is followed by a substrate-induced conformational change step, ES in equilibrium ES. At pH 7.0 and 15 degrees C, the association constants for the direct binding (K1) of ADP to MnE1.0 and of Pi to MnE1.0ADP are 3.9 X 10(4) and 2.28 X 10(2) M(-1), respectively. The association constant for the direct binding of ADP to MnE1.0Pi is 2.3 X 10(4) M(-1) at pH 7.0 and 19 degrees C. The deltaG degrees for the substrate-induced conformational step are -3.5 and -1.3 kcal mol(-1) due to ADP binding to MnE1.0Pi and MnE1.0, respectively, and -1.4 kcal mol(-1) due to Pi binding to MnE1.0ADP. Rate constants, k2 and k(-2), for the isomerization step are: 90 and 9.5 s(-1) for ADP binding to MnE1.0, 440 and 0.36 s(-1) for ADP binding to MnE1.0Pi, and 216 and 1.8 s(-1) for Pi binding to MnE1.0ADP. Due to low substrate affinity, the association constant for direct Pi binding to MnE1.0 was roughly estimated to be 230 M(-1) and k2 = 750 s(-1), k(-2) = 250 s(-1). At 9 degrees C and pH 7.0, the estimated association constants for the direct ADP binding to MgE1.0 and MgE1.0 Pi are 1.8 X 10(4) and 1.6 X 10(4) M(-1), respectively; and the rate constants for the isomerization step associated with the corresponding reaction are k2 = 550 s(-1), k(-2) = 500 s(-1), and k2 = 210 s(-1), k(-2) = 100 s(-1). From the kinetic analysis it is evident that the inability of Mn2+ to support biosynthetic activity of the unadenylylated enzyme is due to the slow rate of ADP release from the MnE1.0PiADP complex. In contrast the large k(-2) obtained for ADP release from the MgE1.0ADP or MgE1.0PiADP complex indicates that this step is not rate limiting in the biosynthesis of glutamine since the k catalysis obtained under the same conditions is 7.2 s(-1). | Mechanistic studies of glutamine synthetase from Escherichia coli: kinetics of ADP and orthophosphate binding to the unadenylylated enzyme. The kinetics of protein fluorescence change exhibited by ADP or orthophosphate addition to the Mg2+-or Mn2+-activated unadenylylated glutamine synthetase from Escherichia coli were studied. The kinetic patterns of these reactions are incompatible with a simple bimolecular binding process and a mechanism which required protein isomerization prior to substrate binding. They are consistent with a mechanism in which direct substrate binding is followed by a substrate-induced conformational change step, ES in equilibrium ES. At pH 7.0 and 15 degrees C, the association constants for the direct binding (K1) of ADP to MnE1.0 and of Pi to MnE1.0ADP are 3.9 X 10(4) and 2.28 X 10(2) M(-1), respectively. The association constant for the direct binding of ADP to MnE1.0Pi is 2.3 X 10(4) M(-1) at pH 7.0 and 19 degrees C. The deltaG degrees for the substrate-induced conformational step are -3.5 and -1.3 kcal mol(-1) due to ADP binding to MnE1.0Pi and MnE1.0, respectively, and -1.4 kcal mol(-1) due to Pi binding to MnE1.0ADP. Rate constants, k2 and k(-2), for the isomerization step are: 90 and 9.5 s(-1) for ADP binding to MnE1.0, 440 and 0.36 s(-1) for ADP binding to MnE1.0Pi, and 216 and 1.8 s(-1) for Pi binding to MnE1.0ADP. Due to low substrate affinity, the association constant for direct Pi binding to MnE1.0 was roughly estimated to be 230 M(-1) and k2 = 750 s(-1), k(-2) = 250 s(-1). At 9 degrees C and pH 7.0, the estimated association constants for the direct ADP binding to MgE1.0 and MgE1.0 Pi are 1.8 X 10(4) and 1.6 X 10(4) M(-1), respectively; and the rate constants for the isomerization step associated with the corresponding reaction are k2 = 550 s(-1), k(-2) = 500 s(-1), and k2 = 210 s(-1), k(-2) = 100 s(-1). From the kinetic analysis it is evident that the inability of Mn2+ to support biosynthetic activity of the unadenylylated enzyme is due to the slow rate of ADP release from the MnE1.0PiADP complex. In contrast the large k(-2) obtained for ADP release from the MgE1.0ADP or MgE1.0PiADP complex indicates that this step is not rate limiting in the biosynthesis of glutamine since the k catalysis obtained under the same conditions is 7.2 s(-1). | [
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PMID:5114 | Nicotinamide adenine dinucleotide phosphate linked isocitrate dehydrogenase. Catalytic activation by the reduced coenzyme product of the reaction. | The oxidative decarboxylation of D-isocitrate catalyzed by NADP-linked isocitrate dehydrogenase is activated by NADPH, the product of the reaction. We analyzed the autocatalytic behavior exhibited by the enzyme during the steady-state kinetics. NADP acts as a competitive inhibitor toward NADPH in the catalytic activation. In a large concentration range of the reduced and oxidized coenzymes, the activity of the enzyme is proportional to the ratio (NADPH)/(NADP). The results are compared with the results of experiments done with other NADP-linked decarboxylating dehydrogenases. Two different models are presented in order to explain the mechanism of action of isocitrate dehydrogenase, according to our data. | Nicotinamide adenine dinucleotide phosphate linked isocitrate dehydrogenase. Catalytic activation by the reduced coenzyme product of the reaction. The oxidative decarboxylation of D-isocitrate catalyzed by NADP-linked isocitrate dehydrogenase is activated by NADPH, the product of the reaction. We analyzed the autocatalytic behavior exhibited by the enzyme during the steady-state kinetics. NADP acts as a competitive inhibitor toward NADPH in the catalytic activation. In a large concentration range of the reduced and oxidized coenzymes, the activity of the enzyme is proportional to the ratio (NADPH)/(NADP). The results are compared with the results of experiments done with other NADP-linked decarboxylating dehydrogenases. Two different models are presented in order to explain the mechanism of action of isocitrate dehydrogenase, according to our data. | [
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PMID:5115 | Role of mannosyl lipid intermediate in the synthesis of Neurospora crassa glycoproteins. | Particulate membrane preparations from Neurospora crassa incorporated mannose from GDP-[14C] mannose into endogenous lipid and particulate protein acceptors. Synthesis of the mannosyl lipid is reversible in the presence of GDP. Chemical and chromatographic characterization of the mannosyl lipid suggest that it is a mannosylphosphorylpolyisoprenol. The other endogenous acceptor was precipitated by trichloracetic acid. Gel filtration and electrophoresis studies before and after treatment with proteolytic enzymes indicate that the second acceptor is a glycoprotein(s). beta Elimination studies on the mannosyl protein formed from GDP-[14C] mannose with Mg2+ in the reaction mixture or formed from mannosyl lipid indicate thad with the peptide chain. Several lines of evidence indicate that in Neurospora crassa the mannosyl lipid is an obligatory intermediate in the in vitro mannosylation of the protein. (a) At 15 degrees C the initial formation of the mannosyl lipid is faster than the initial formation of the mannosyl protein. (b) Exogenous partially purified mannosyl lipid can function as a mannosyl donor for the synthesis of the mannosyl protein. This reaction was also dependent on a divalent metal. The rate of this reaction was optimal at a concentration of Triton X-100 which effectively inhibited the transfer of mannose from GDP-[14C] mannose to lipid and protein, indicating that GDP-mannose was not an intermediate in the transfer of mannose from lipid to protein. The mannosyl protein formed in this reaction was indistinguishable by several criteria from the mannosyl protein formed from GDP-[14C] mannose and Mg2+. (c) The effect of a chase with an excess of unlabeled GDP-mannose on the incorporation of mannose into endogenous acceptors was immediate cessation of the synthesis and subsequent turnover of the mannosyl lipid; in contrast, however, incorporation of mannose into protein continued and was proportional to the loss of mannose from the mannosyl lipid. | Role of mannosyl lipid intermediate in the synthesis of Neurospora crassa glycoproteins. Particulate membrane preparations from Neurospora crassa incorporated mannose from GDP-[14C] mannose into endogenous lipid and particulate protein acceptors. Synthesis of the mannosyl lipid is reversible in the presence of GDP. Chemical and chromatographic characterization of the mannosyl lipid suggest that it is a mannosylphosphorylpolyisoprenol. The other endogenous acceptor was precipitated by trichloracetic acid. Gel filtration and electrophoresis studies before and after treatment with proteolytic enzymes indicate that the second acceptor is a glycoprotein(s). beta Elimination studies on the mannosyl protein formed from GDP-[14C] mannose with Mg2+ in the reaction mixture or formed from mannosyl lipid indicate thad with the peptide chain. Several lines of evidence indicate that in Neurospora crassa the mannosyl lipid is an obligatory intermediate in the in vitro mannosylation of the protein. (a) At 15 degrees C the initial formation of the mannosyl lipid is faster than the initial formation of the mannosyl protein. (b) Exogenous partially purified mannosyl lipid can function as a mannosyl donor for the synthesis of the mannosyl protein. This reaction was also dependent on a divalent metal. The rate of this reaction was optimal at a concentration of Triton X-100 which effectively inhibited the transfer of mannose from GDP-[14C] mannose to lipid and protein, indicating that GDP-mannose was not an intermediate in the transfer of mannose from lipid to protein. The mannosyl protein formed in this reaction was indistinguishable by several criteria from the mannosyl protein formed from GDP-[14C] mannose and Mg2+. (c) The effect of a chase with an excess of unlabeled GDP-mannose on the incorporation of mannose into endogenous acceptors was immediate cessation of the synthesis and subsequent turnover of the mannosyl lipid; in contrast, however, incorporation of mannose into protein continued and was proportional to the loss of mannose from the mannosyl lipid. | [
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PMID:5116 | Histidine ammonia-lyase from rat liver. Purification, properties, and inhibition by substrate analogues. | Histidine ammonia-lyase (EC 4.3.1.3) from rat liver was purified more than 250-fold to near homogeneity. Electrophoretic determinations indicated a native molecular weight of approximately 200,000. The enzyme has a pH optimum of approximately pH 8.5. The minimum Km for L-histidine was 0.5 mM at pH 9.0. The Michaelis constant in the physiological pH range was, however, more than 2.0 mM. D-alpha-hydrazinoimidazolylpropionic acid was found to be a potent competitive inhibitor of liver histidine ammonia-lyase (Kis=75 muM); the L enantiomer of this compound was less effective in this regard. The enzyme was also inhibited competitively by L-histidine hydroxamate (Kis=0.4 mM), and to a lesser extent by L-histidinol, D-histidine, and glycine. Failure of a wide variety of other histidine analogues to inhibit the enzyme substantially indicates high specificity of the active site for L-histidine. No alternate substrates were identified for the enzyme. DL-alpha-Hydrazinophenylpropionic acid, the alpha-hydrzino analogue of phenylalanine, was similarly shown to be a very potent competitive inhibitor of a mechanistically similar L-phenylalanine ammonia-lyase purified from Rhodotorula glutinis. The properties of histidine ammonia-lyase from rat liver differ significantly from those of the enzyme from Pseudomonas fluorescens which has been studied most extensively to date. | Histidine ammonia-lyase from rat liver. Purification, properties, and inhibition by substrate analogues. Histidine ammonia-lyase (EC 4.3.1.3) from rat liver was purified more than 250-fold to near homogeneity. Electrophoretic determinations indicated a native molecular weight of approximately 200,000. The enzyme has a pH optimum of approximately pH 8.5. The minimum Km for L-histidine was 0.5 mM at pH 9.0. The Michaelis constant in the physiological pH range was, however, more than 2.0 mM. D-alpha-hydrazinoimidazolylpropionic acid was found to be a potent competitive inhibitor of liver histidine ammonia-lyase (Kis=75 muM); the L enantiomer of this compound was less effective in this regard. The enzyme was also inhibited competitively by L-histidine hydroxamate (Kis=0.4 mM), and to a lesser extent by L-histidinol, D-histidine, and glycine. Failure of a wide variety of other histidine analogues to inhibit the enzyme substantially indicates high specificity of the active site for L-histidine. No alternate substrates were identified for the enzyme. DL-alpha-Hydrazinophenylpropionic acid, the alpha-hydrzino analogue of phenylalanine, was similarly shown to be a very potent competitive inhibitor of a mechanistically similar L-phenylalanine ammonia-lyase purified from Rhodotorula glutinis. The properties of histidine ammonia-lyase from rat liver differ significantly from those of the enzyme from Pseudomonas fluorescens which has been studied most extensively to date. | [
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PMID:5117 | Partial denaturation of mouse DNA in preparative CsCl density gradients at alkaline pH. | A new technique--partial denaturation of DNA in equilibrium CsCl density gradients at pH 11.4--is used to determine the distribution of intermediate states in the melting of mouse DNA. When the technique is applied in the preparative ultracentrifuge, the DNA is fractionated according to stability. Neutralization of the partially denatured fractions results in the recovery of most of the DNA in its native form. The individual fractions are more homogeneous than the total DNA: they have decreased density heterogeneity (smaller band widths), neutral CsCl buoyant densities that differ from the average, and more homogeneous melting profiles with melting temperatures that differ from the average. | Partial denaturation of mouse DNA in preparative CsCl density gradients at alkaline pH. A new technique--partial denaturation of DNA in equilibrium CsCl density gradients at pH 11.4--is used to determine the distribution of intermediate states in the melting of mouse DNA. When the technique is applied in the preparative ultracentrifuge, the DNA is fractionated according to stability. Neutralization of the partially denatured fractions results in the recovery of most of the DNA in its native form. The individual fractions are more homogeneous than the total DNA: they have decreased density heterogeneity (smaller band widths), neutral CsCl buoyant densities that differ from the average, and more homogeneous melting profiles with melting temperatures that differ from the average. | [
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PMID:5118 | Laser Raman spectroscopic studies of the thermal unfolding of ribonuclease A. | The reversible thermal denaturation of bovine pancreatic ribonuclease A at pH 5 in 0.1 M NaCl over the range 32-70 degrees C as studied by Raman spectroscopy proceeds in a gradual manner consistent with a stepwise unfolding process rather than as a transition between two states. Conversion of residues from helical or pleated-sheet geometry to some intermediate geometry, as followed by means of the amide I and III lines, reveals that substantial amounts of the helical and pleated-sheet conformations remain at 70 degrees C. Changes in the strength of hydrogen bonding by the tyrosyl residues are indicated by the intensity ratio of the doublet at 830-850 cm(-1) and changes in the geometry of the disulfide bridges by the frequency and half-width of the Raman line near 510 cm(-1) due to the S-S vibration. Vibrations of C-S bonds in the methionines and cystines are used to monitor conformational changes in these residues. While there are small quantitative differences in temperature dependence among these probes, all agree in placing the malting temperature at or near 62 degrees C. The Raman data are quantitatively consistent with the six-stage scheme of unfolding of A.W. Burgess and H.A. Scheraga [(1975), J. Theor, Biol. 53, 403], except that no change in the environment of the tyrosines is seen until 45 degrees C. | Laser Raman spectroscopic studies of the thermal unfolding of ribonuclease A. The reversible thermal denaturation of bovine pancreatic ribonuclease A at pH 5 in 0.1 M NaCl over the range 32-70 degrees C as studied by Raman spectroscopy proceeds in a gradual manner consistent with a stepwise unfolding process rather than as a transition between two states. Conversion of residues from helical or pleated-sheet geometry to some intermediate geometry, as followed by means of the amide I and III lines, reveals that substantial amounts of the helical and pleated-sheet conformations remain at 70 degrees C. Changes in the strength of hydrogen bonding by the tyrosyl residues are indicated by the intensity ratio of the doublet at 830-850 cm(-1) and changes in the geometry of the disulfide bridges by the frequency and half-width of the Raman line near 510 cm(-1) due to the S-S vibration. Vibrations of C-S bonds in the methionines and cystines are used to monitor conformational changes in these residues. While there are small quantitative differences in temperature dependence among these probes, all agree in placing the malting temperature at or near 62 degrees C. The Raman data are quantitatively consistent with the six-stage scheme of unfolding of A.W. Burgess and H.A. Scheraga [(1975), J. Theor, Biol. 53, 403], except that no change in the environment of the tyrosines is seen until 45 degrees C. | [
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PMID:5119 | Hydrogen ion titration of horse heart ferricytochrome c. | Continuous hydrogen ion titration curves of deionized solutions of horse heart ferricytochrome c have been obtained at 25 degrees C. at a constant ionic strength of 0.10 from pH 3.0 to 11.0. Titration of the oxidized protein in KCl required 28.4 equiv over that pH range, and a small hysteresis between the forward and reverse limbs was displayed. The Linderstrom-Lang approximation, which takes into account electrostatic interactions between charged groups on the protein surface, was used in a computer simulation program to analyze the forward and reverse limbs of the titration curve separately. The results indicated 1 alpha-, 12 beta- and gamma-, and 1 heme propionic carboxylic, 1 imidazole, 1 phenolic, and 18 epsilon-amino residues appear to titrate normally. Variations in the electrostatic interaction factor omega suggest conformational changes in the protein at the extremes of pH, although the relationship of the variations in omega to the magnitude of the conformational changes does not appear to be strictly quantitative for cytochrome c. These results show the acid-base behavior of cytochrome c to be complex in nature, and suggest that the Lindenstrom-Lang model may not be adequate for cytochrome c. | Hydrogen ion titration of horse heart ferricytochrome c. Continuous hydrogen ion titration curves of deionized solutions of horse heart ferricytochrome c have been obtained at 25 degrees C. at a constant ionic strength of 0.10 from pH 3.0 to 11.0. Titration of the oxidized protein in KCl required 28.4 equiv over that pH range, and a small hysteresis between the forward and reverse limbs was displayed. The Linderstrom-Lang approximation, which takes into account electrostatic interactions between charged groups on the protein surface, was used in a computer simulation program to analyze the forward and reverse limbs of the titration curve separately. The results indicated 1 alpha-, 12 beta- and gamma-, and 1 heme propionic carboxylic, 1 imidazole, 1 phenolic, and 18 epsilon-amino residues appear to titrate normally. Variations in the electrostatic interaction factor omega suggest conformational changes in the protein at the extremes of pH, although the relationship of the variations in omega to the magnitude of the conformational changes does not appear to be strictly quantitative for cytochrome c. These results show the acid-base behavior of cytochrome c to be complex in nature, and suggest that the Lindenstrom-Lang model may not be adequate for cytochrome c. | [
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PMID:5120 | Isolation of brain endopeptidases: influence of size and sequence of substrates structurally related to bradykinin. | Two thiol-activated endopeptidases with pH optima near pH 7.5 were isolated from the supernatant fraction of rabbit brain homogenates by DEAE-cellulose chromatography, gel filtration and isoelectrofocusing. Peptide bond hydrolysis was measured quantitatively by ion-exchange chromatography with an amino acid analyzer. Brain kininase A hydrolyzes the Phe5-Ser6 peptide bond in bradykinin (Bk), Arg1-Pro2-Pro3-Gly4-Phe5-Ser6-Pro7-Phe8-Arg9. It is isoelectric near pH 5.2 and has a molecular weight of approximately 71 000. The enzyme also hydrolyzes the Phe-Ser peptide bond in Lys-Bk, Met-Lys-Bk, des-Arg1-Bk, Lys9-Bk, Pro-Gly-Phe-Ser-Pro-Phe-Arg, and Gly-Pro-Phe-Ser-Pro-Phe-Arg, but does not hydrolyze (0.1%) this bond in des-Phe8-Arg9-Bk. Brain kininase B hydrolyzes the Pro7-Phe8 peptide bond in Bk. It is isoelectric at pH 4.9 and has a molecular weight of approximately 68 000. Brain kininase B also hydrolyzes the Pro-Phe bond in Lys-Bk, Met-Lys-Bk, Lys9-Bk, Ser-Pro-Phe-Arg, and Phe-Ser-Pro-Arg. Pretreatment of denatured kininogen with brain kininase A or B did not reduce the amount of trypsin-releasable Bk from this precursor protein, indicating that the Bk sequence, when part of a large protein, is not a substrate for either enzyme. However, kininase A and B hydrolyze the octadecapeptide Gly-Leu-Met-Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Val-Gin-Val. The data show that a large part of the C-terminal portion of bradykinin is important for the brain kininase A activity and, for both enzymes, the size of the peptide and presumably the residues adjacent to the scissle bond are important in determining the rate of peptide bond hydrolysis by these endopeptidases. | Isolation of brain endopeptidases: influence of size and sequence of substrates structurally related to bradykinin. Two thiol-activated endopeptidases with pH optima near pH 7.5 were isolated from the supernatant fraction of rabbit brain homogenates by DEAE-cellulose chromatography, gel filtration and isoelectrofocusing. Peptide bond hydrolysis was measured quantitatively by ion-exchange chromatography with an amino acid analyzer. Brain kininase A hydrolyzes the Phe5-Ser6 peptide bond in bradykinin (Bk), Arg1-Pro2-Pro3-Gly4-Phe5-Ser6-Pro7-Phe8-Arg9. It is isoelectric near pH 5.2 and has a molecular weight of approximately 71 000. The enzyme also hydrolyzes the Phe-Ser peptide bond in Lys-Bk, Met-Lys-Bk, des-Arg1-Bk, Lys9-Bk, Pro-Gly-Phe-Ser-Pro-Phe-Arg, and Gly-Pro-Phe-Ser-Pro-Phe-Arg, but does not hydrolyze (0.1%) this bond in des-Phe8-Arg9-Bk. Brain kininase B hydrolyzes the Pro7-Phe8 peptide bond in Bk. It is isoelectric at pH 4.9 and has a molecular weight of approximately 68 000. Brain kininase B also hydrolyzes the Pro-Phe bond in Lys-Bk, Met-Lys-Bk, Lys9-Bk, Ser-Pro-Phe-Arg, and Phe-Ser-Pro-Arg. Pretreatment of denatured kininogen with brain kininase A or B did not reduce the amount of trypsin-releasable Bk from this precursor protein, indicating that the Bk sequence, when part of a large protein, is not a substrate for either enzyme. However, kininase A and B hydrolyze the octadecapeptide Gly-Leu-Met-Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Val-Gin-Val. The data show that a large part of the C-terminal portion of bradykinin is important for the brain kininase A activity and, for both enzymes, the size of the peptide and presumably the residues adjacent to the scissle bond are important in determining the rate of peptide bond hydrolysis by these endopeptidases. | [
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PMID:5121 | Glucose-6-phosphate dehydrogenase from brewers' yeast. The effects of pH and temperature on the steady-state kinetic parameters of the two-chain protein species. | A systematic study has been made of the pH- and temperature-dependency of the steady-state kinetic parameters of the stabilized two-subunit enzyme species of glucose-6-phosphate dehydrogenase, in the absence of superimposed association-dissociation reactions. The Vmax(app) data obtained in several buffers between pH 5 and 10 and at 18-32 degrees C lead to the postulate that at least two sets of protonic equilibria may govern the catalysis (one near pH 5.7 AT 25 DEGREES C and another near pH 9.2); furthermore, two pathways for product formation (i.e., two Vmax's) appear to be required to explain the biphasic nature of the log Vmax(app) vs. pH curves, with Vmax(basic) greater than Vmax(acidic + neutral). Of the several buffers explored, either a uniform degree of interaction or a minimal degree of buffer species interaction could be assessed from the enthalpy changes associated with the derived values for ionization constants attributed to the protonic equilibria in the enzyme-substrates ternary complexes for the case of Tris-acetate-EDTA buffers, at constant ionic strength. With the selection of this buffer at 0.1 (T/2) and at 25 and 32 degrees C, a self-consistent kinetic mechanism has emerged which allows for the random binding of the two fully ionized substrates to the enzyme via two major pathways, and product formation by both E-A--B- and HE-A--B-. As before (Kuby et al. Arch. Biochem, Biophys. 165, 153-178, 1974), a quasi-equilibrium is presumed, with rate-limiting steps (k + 5 and k + 5') at the interconversion of the ternary complexes. Values for the two sets of protonic equilibria defined by this mechanism (viz., pKk, pKH2 for the first ionizations, and pKk', pKH' for the second) could then be estimated. From their numerical values (e.g., at 25 degrees C: pKK = 5.7 PKH2 = 5.2; and pKK' = 9.1, PKH' = 8.2) and from the values for delta H degrees ioniz (e.g., delta H degrees pKK APPROXIMATELY 5.1 KCAL/MOL; DELTA H degrees pKK' APPROXIMATELY 11 KCAL/MOL), A POSTULATE IS PRESENTED WHICH ATTRIBUTES THESE Acid dissociation constants to an imidazole and epsilon-amino group, respectively. | Glucose-6-phosphate dehydrogenase from brewers' yeast. The effects of pH and temperature on the steady-state kinetic parameters of the two-chain protein species. A systematic study has been made of the pH- and temperature-dependency of the steady-state kinetic parameters of the stabilized two-subunit enzyme species of glucose-6-phosphate dehydrogenase, in the absence of superimposed association-dissociation reactions. The Vmax(app) data obtained in several buffers between pH 5 and 10 and at 18-32 degrees C lead to the postulate that at least two sets of protonic equilibria may govern the catalysis (one near pH 5.7 AT 25 DEGREES C and another near pH 9.2); furthermore, two pathways for product formation (i.e., two Vmax's) appear to be required to explain the biphasic nature of the log Vmax(app) vs. pH curves, with Vmax(basic) greater than Vmax(acidic + neutral). Of the several buffers explored, either a uniform degree of interaction or a minimal degree of buffer species interaction could be assessed from the enthalpy changes associated with the derived values for ionization constants attributed to the protonic equilibria in the enzyme-substrates ternary complexes for the case of Tris-acetate-EDTA buffers, at constant ionic strength. With the selection of this buffer at 0.1 (T/2) and at 25 and 32 degrees C, a self-consistent kinetic mechanism has emerged which allows for the random binding of the two fully ionized substrates to the enzyme via two major pathways, and product formation by both E-A--B- and HE-A--B-. As before (Kuby et al. Arch. Biochem, Biophys. 165, 153-178, 1974), a quasi-equilibrium is presumed, with rate-limiting steps (k + 5 and k + 5') at the interconversion of the ternary complexes. Values for the two sets of protonic equilibria defined by this mechanism (viz., pKk, pKH2 for the first ionizations, and pKk', pKH' for the second) could then be estimated. From their numerical values (e.g., at 25 degrees C: pKK = 5.7 PKH2 = 5.2; and pKK' = 9.1, PKH' = 8.2) and from the values for delta H degrees ioniz (e.g., delta H degrees pKK APPROXIMATELY 5.1 KCAL/MOL; DELTA H degrees pKK' APPROXIMATELY 11 KCAL/MOL), A POSTULATE IS PRESENTED WHICH ATTRIBUTES THESE Acid dissociation constants to an imidazole and epsilon-amino group, respectively. | [
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PMID:5122 | A quantitation of the factors which affect the hydrolase and transgalactosylase activities of beta-galactosidase (E. coli) on lactose. | A study was implemented to quantitate the hydrolase and transgalactosylase activities of beta-galactosidase (E. coli) with lactose as the substrate and to investigate various factors which affect these activities. At low lactose concentrations the rate of galactose production was equal to the rate of glucose production. The rate of galactose production relative to glucose, however, dropped dramatically at lactose concentrations higher than 0.05 M and production of trisaccharides and tetrasaccharides began (galactose/glucose ratios of about 2:1 and 3:1, respectively, were found for these two types of oligosaccharides). At least five different trissacharides were formed and their patterns of formation showed that they probably utilized both lactose and allolactose as galactosyl acceptors. Allolactose was produced in amounts proportional to glucose at all lactose concentrations (ratios of allolactose/glucose were about 0.88). Analyses of various data, including a reaction analyzed at very early times, showed that the major means of production of allolactose (and the only means initially) was the direct enzymatic transfer of galactose from the 4 position to the 6 position of the glucose moiety of lactose without prior release of glucose from the enzyme. It was shown, however, that allolactose could also be formed in significant quantities by the transfer of galactose to the 6 position of free glucose, and also by hydrolysis of preformed trisaccharide. A mechanism which fits the initial velocity data was proposed in which the steps involving the formation of an enzyme-gallactose-glucose complex, the formation and breakage of allolactose on the enzyme, and the release of glucose all seem to be of roughly equal magnitude and rate determining. Various factors affected the amounts of transgalactosylase and hydrolase activities occurring. At high pH values (greater than 7.8) the transgalactosylase/hydrolyase activity ratio increased dramatically while it decreased at low pH values (less than 6.0). At mid pH values the ratio was essentially constant. The absence of Mg2+ caused a large decrease in the transgalactosylase/hydrolase activity ratio while the absence of all but traces of Na+ or K+ had no effect. The anomeric configuration of lactose altered the transgalactosylase/hydrolase activity ratios, alpha-Lactose resulted in a decrease of allolactose production (transgalactosylase activity) relative to hydrolase activities (glucose production) while beta-lactose had the opposite effect. | A quantitation of the factors which affect the hydrolase and transgalactosylase activities of beta-galactosidase (E. coli) on lactose. A study was implemented to quantitate the hydrolase and transgalactosylase activities of beta-galactosidase (E. coli) with lactose as the substrate and to investigate various factors which affect these activities. At low lactose concentrations the rate of galactose production was equal to the rate of glucose production. The rate of galactose production relative to glucose, however, dropped dramatically at lactose concentrations higher than 0.05 M and production of trisaccharides and tetrasaccharides began (galactose/glucose ratios of about 2:1 and 3:1, respectively, were found for these two types of oligosaccharides). At least five different trissacharides were formed and their patterns of formation showed that they probably utilized both lactose and allolactose as galactosyl acceptors. Allolactose was produced in amounts proportional to glucose at all lactose concentrations (ratios of allolactose/glucose were about 0.88). Analyses of various data, including a reaction analyzed at very early times, showed that the major means of production of allolactose (and the only means initially) was the direct enzymatic transfer of galactose from the 4 position to the 6 position of the glucose moiety of lactose without prior release of glucose from the enzyme. It was shown, however, that allolactose could also be formed in significant quantities by the transfer of galactose to the 6 position of free glucose, and also by hydrolysis of preformed trisaccharide. A mechanism which fits the initial velocity data was proposed in which the steps involving the formation of an enzyme-gallactose-glucose complex, the formation and breakage of allolactose on the enzyme, and the release of glucose all seem to be of roughly equal magnitude and rate determining. Various factors affected the amounts of transgalactosylase and hydrolase activities occurring. At high pH values (greater than 7.8) the transgalactosylase/hydrolyase activity ratio increased dramatically while it decreased at low pH values (less than 6.0). At mid pH values the ratio was essentially constant. The absence of Mg2+ caused a large decrease in the transgalactosylase/hydrolase activity ratio while the absence of all but traces of Na+ or K+ had no effect. The anomeric configuration of lactose altered the transgalactosylase/hydrolase activity ratios, alpha-Lactose resulted in a decrease of allolactose production (transgalactosylase activity) relative to hydrolase activities (glucose production) while beta-lactose had the opposite effect. | [
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PMID:5123 | The major sialoglycoprotein of the human erythrocyte membrane. Release with a non-ionic detergent and purification. | The major sialoglycoprotein of the human erythrocyte membrane has been selectively released by the non-ionic detergent Tween 20 and further purified in detergent-free buffers by hydroxyapatite chromatography and, finally, by hydrophobic interaction chromatography on pentyl-Sepharose. The purified glycoprotein shows one main zone, PAS-1, and up to three minor zones after staining both for protein and carbohydrate in polyacrylamide gel electrophoresis in the presence of dodecyl sulfate. The relative staining intensities are concentration dependent. When the purified glycoprotein has been heated to 100 degrees C in dodecyl sulfate, more stain appears in the most rapid zone, PAS-2, and less in the slower zones, indicating a disaggregation of oligomeric forms of this glycoprotein, including a dimer, PAS-1. | The major sialoglycoprotein of the human erythrocyte membrane. Release with a non-ionic detergent and purification. The major sialoglycoprotein of the human erythrocyte membrane has been selectively released by the non-ionic detergent Tween 20 and further purified in detergent-free buffers by hydroxyapatite chromatography and, finally, by hydrophobic interaction chromatography on pentyl-Sepharose. The purified glycoprotein shows one main zone, PAS-1, and up to three minor zones after staining both for protein and carbohydrate in polyacrylamide gel electrophoresis in the presence of dodecyl sulfate. The relative staining intensities are concentration dependent. When the purified glycoprotein has been heated to 100 degrees C in dodecyl sulfate, more stain appears in the most rapid zone, PAS-2, and less in the slower zones, indicating a disaggregation of oligomeric forms of this glycoprotein, including a dimer, PAS-1. | [
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PMID:5124 | An electron paramagnetic resonance study of Mn2+ uptake by the chick chorioallantoic membrane. | Mn2+ uptake in the chick chorioallantoic membrane, an embryonic epithelial tissue which transports Ca2+ in vivo was studied using electron paramagnetic resonance (EPR). Mn2+ was used as a paramagnetic analog for Ca2+, since there is evidence that Mn2+ is accumulated by the Ca2+ transport mechanism. After 1.5 h of uptake the EPR spectrum of the Mn2+ in the membrane indicated that 89% of the Mn2+ was in a spin-exchange form, indicating close packing of Mn2+. The Mn2+ spacing was estimated from the line width to be about 4.7 A. The remaining Mn2+ was very likely Mn2+ hexahydrate. At pH 7.4 the spin-exchange spectrum tended to broaden when uptake was inhibited, while at pH 5.0 the spin-exchange spectrum was completely abolished in the presence of inhibitors. The EPR spectrum of Mn2+ in the chorioallantoic membrane had a broader line width than that of Mn2+ in isolated mitochondria, suggesting that in this tissue mitochondria are not directly involved in divalent cation transport. These EPR studies support the concept that divalent cations are sequestered in high concentrations from the rest of the cell contents during transcellular active transport. | An electron paramagnetic resonance study of Mn2+ uptake by the chick chorioallantoic membrane. Mn2+ uptake in the chick chorioallantoic membrane, an embryonic epithelial tissue which transports Ca2+ in vivo was studied using electron paramagnetic resonance (EPR). Mn2+ was used as a paramagnetic analog for Ca2+, since there is evidence that Mn2+ is accumulated by the Ca2+ transport mechanism. After 1.5 h of uptake the EPR spectrum of the Mn2+ in the membrane indicated that 89% of the Mn2+ was in a spin-exchange form, indicating close packing of Mn2+. The Mn2+ spacing was estimated from the line width to be about 4.7 A. The remaining Mn2+ was very likely Mn2+ hexahydrate. At pH 7.4 the spin-exchange spectrum tended to broaden when uptake was inhibited, while at pH 5.0 the spin-exchange spectrum was completely abolished in the presence of inhibitors. The EPR spectrum of Mn2+ in the chorioallantoic membrane had a broader line width than that of Mn2+ in isolated mitochondria, suggesting that in this tissue mitochondria are not directly involved in divalent cation transport. These EPR studies support the concept that divalent cations are sequestered in high concentrations from the rest of the cell contents during transcellular active transport. | [
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PMID:5125 | Spectroscopic studies on the complex formation of suramin with bovine and human serum albumin. | The binding of suramin to bovine and human serum albumin was investigated by gel filtration and spectroscopic measurements. Besides some low-affinity binding sites suramin has, on the bovine serum albumin molecule one and on the human serum albumin molecule two, high-affinity binding sites. Spectroscopic measurements reveal that there are large differences between the albumins in the mechanism of binding to the high-affinity binding sites. Further, it is suggested that high concentrations of suramin provoke an unfolding of the albumin moleculse. In order to explain the unusual behaviour of suramin in connection with the displacement of other ligands from the albumin binding the fluorescence probe 1-anilino-8-naphthalenesulfonic acid (ANS) was employed as a reporter group molecule for fluorescence as well as circular dichroism measurements. By these measurements it could be shown that suramin greatly influences the microorganization of both albumin molecules. In the case of these measurements large differences between bovine and human serum albumin were also found. | Spectroscopic studies on the complex formation of suramin with bovine and human serum albumin. The binding of suramin to bovine and human serum albumin was investigated by gel filtration and spectroscopic measurements. Besides some low-affinity binding sites suramin has, on the bovine serum albumin molecule one and on the human serum albumin molecule two, high-affinity binding sites. Spectroscopic measurements reveal that there are large differences between the albumins in the mechanism of binding to the high-affinity binding sites. Further, it is suggested that high concentrations of suramin provoke an unfolding of the albumin moleculse. In order to explain the unusual behaviour of suramin in connection with the displacement of other ligands from the albumin binding the fluorescence probe 1-anilino-8-naphthalenesulfonic acid (ANS) was employed as a reporter group molecule for fluorescence as well as circular dichroism measurements. By these measurements it could be shown that suramin greatly influences the microorganization of both albumin molecules. In the case of these measurements large differences between bovine and human serum albumin were also found. | [
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PMID:5126 | Interactions between hemoglobin and organic phosphates investigated with 31P nuclear magnetic resonance spectroscopy and ultrafiltration. | 1. The chemical shifts (delta) of the phosphates of 2,3-diphosphoglycerate and adenosine triphosphate (ATP) were determined by phosphorus nuclear magnetic resonance (31P NMR) spectroscopy and were found to be displaced downfield following the addition of hemoglobin (3 mM) to a solution of either diphosphoglycerate (5 mM) or ATP (1 mM). 2. The binding of these compounds to hemoglobin was also determined by membrane ultrafiltration. A direct relationship was observed between the change in chemical shift ((delta delta) of the 2-P and 3-P of diphosphoglycerate and the percent diphosphoglycerate bound, when the latter was varied by altering pH, oxygenation state, or total diphosphoglycerate concentration. 3. In comparable studies with ATP binding, a linear relationship between the delta delta values of the gamma-, beta-, and alpha-P of ATP and the percent of ATP bound was not observed when the data from all of the experiments were plotted. NMR signals were not detectible in deoxyhemoglobin solutions containing 1 mM ATP but were seen in solutions containing 3.8 mM ATP. 4. The results indicate that 31P NMR spectroscopy is a promising tool for investigating organic phosphate interactions with hemoglobin. | Interactions between hemoglobin and organic phosphates investigated with 31P nuclear magnetic resonance spectroscopy and ultrafiltration. 1. The chemical shifts (delta) of the phosphates of 2,3-diphosphoglycerate and adenosine triphosphate (ATP) were determined by phosphorus nuclear magnetic resonance (31P NMR) spectroscopy and were found to be displaced downfield following the addition of hemoglobin (3 mM) to a solution of either diphosphoglycerate (5 mM) or ATP (1 mM). 2. The binding of these compounds to hemoglobin was also determined by membrane ultrafiltration. A direct relationship was observed between the change in chemical shift ((delta delta) of the 2-P and 3-P of diphosphoglycerate and the percent diphosphoglycerate bound, when the latter was varied by altering pH, oxygenation state, or total diphosphoglycerate concentration. 3. In comparable studies with ATP binding, a linear relationship between the delta delta values of the gamma-, beta-, and alpha-P of ATP and the percent of ATP bound was not observed when the data from all of the experiments were plotted. NMR signals were not detectible in deoxyhemoglobin solutions containing 1 mM ATP but were seen in solutions containing 3.8 mM ATP. 4. The results indicate that 31P NMR spectroscopy is a promising tool for investigating organic phosphate interactions with hemoglobin. | [
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PMID:5127 | Contact-shifted resonances in the 1H NMR spectra of cytochrome b5. Resonance identification and spin density distribution in the heme group. | This paper describes the identification of some of the contact-shifted resonances in the 1H NMR spectrum of low spin ferric cytochrome b5. In these experiments comparison with cytochrome b5 which had been reconstituted with deuteroheme IX played an important role. NMR techniques used include double resonance experiments, line width analyses, and studies of the pH-dependence of the 1H NMR chemical shifts. The electronic heme structure derived from these resonance assignments is characterized by a highly anisotropic spin density distribution. This anisotropy is most strikingly manifested in the resonances of the vinyl and propionic acid substituents of the protoheme IX. The experiments described in this paper further revealed the coexistence in aqueous solutions of two different molecular species of cytochrome b5, which can be simultaneously observed in the regions of the 1H NMR spectrum which contain the largely contact-shifted resonances. | Contact-shifted resonances in the 1H NMR spectra of cytochrome b5. Resonance identification and spin density distribution in the heme group. This paper describes the identification of some of the contact-shifted resonances in the 1H NMR spectrum of low spin ferric cytochrome b5. In these experiments comparison with cytochrome b5 which had been reconstituted with deuteroheme IX played an important role. NMR techniques used include double resonance experiments, line width analyses, and studies of the pH-dependence of the 1H NMR chemical shifts. The electronic heme structure derived from these resonance assignments is characterized by a highly anisotropic spin density distribution. This anisotropy is most strikingly manifested in the resonances of the vinyl and propionic acid substituents of the protoheme IX. The experiments described in this paper further revealed the coexistence in aqueous solutions of two different molecular species of cytochrome b5, which can be simultaneously observed in the regions of the 1H NMR spectrum which contain the largely contact-shifted resonances. | [
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PMID:5128 | Cooperative reactions of poly-L-lysine-heme complex with molecular oxygen, carbon monoxide, or cyanide ion. | The interaction of the alpha-helical poly-L-lysine-heme complex with molecular oxygen, carbon monoxide, or cyanide ion was studied. Binding equilibrium curve and activation parameters for the reactions were determined. Sigmoid responses were observed for the absorption of molecular oxygen or carbon monoxide by the complex and the cooperative parameter was found to be 2.1. This indicated a cooperative interaction between hemes situated on a cylindrical alpha-helix of poly-L-lysine. But those of other polymer-ligand-heme complexes were 1.0. The cooperative reaction mechanism, in which an alpha-helical poly-L-lysine plays an important role, was suggested. | Cooperative reactions of poly-L-lysine-heme complex with molecular oxygen, carbon monoxide, or cyanide ion. The interaction of the alpha-helical poly-L-lysine-heme complex with molecular oxygen, carbon monoxide, or cyanide ion was studied. Binding equilibrium curve and activation parameters for the reactions were determined. Sigmoid responses were observed for the absorption of molecular oxygen or carbon monoxide by the complex and the cooperative parameter was found to be 2.1. This indicated a cooperative interaction between hemes situated on a cylindrical alpha-helix of poly-L-lysine. But those of other polymer-ligand-heme complexes were 1.0. The cooperative reaction mechanism, in which an alpha-helical poly-L-lysine plays an important role, was suggested. | [
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PMID:5129 | Interaction of serum albumin with normal and sickle hemoglobins. | The stability of oxyhemoglobin S during mechanical shaking was enhanced by the addition of human serum albumin. The stabilizing effect was maximum when the concentration of serum albumin approached that of oxyhemoglobin, suggesting a molecular level interaction between them. The effects of serum albumin on oxyhemoglobin A were essentially similar to those on oxyhemoglobin S. Deoxy- and methemoglobins were also stabilized by serum albumin. The addition of human serum albumin to a solution containing sickle cell oxyhemoglobin slowly formed a compound which had an absorbance peak at 620 nm. After purification by Sephadex G-200 column chromatography, this compound was identified as methemalbumin. Comparison of the rates of formation of methemalbumin from hemoglobin with various ligand states and human serum albumin showed that the rate of formation from hemichrome was much faster than from met-, oxy- and deoxyhemoglobin. About 60% of the heme was transferred from hemichrome to albumin when the mixture was kept standing at room temperature for 5 min, in contrast to only 5% from methemoglobin. This result suggests that hemichrome, rather than methemoglobin, is the intermediate in the formation of methemalbumin from oxyhemoglobin and human serum albumin. This hypothesis is supported by the finding that the rate of formation of methemalbumin was faster at alkaline pH values than at acid pH values. Serum albumin from various animal sources showed different stabilizing effects. The formation of methemalbumin from these animal albumins was far less than that from human albumin. | Interaction of serum albumin with normal and sickle hemoglobins. The stability of oxyhemoglobin S during mechanical shaking was enhanced by the addition of human serum albumin. The stabilizing effect was maximum when the concentration of serum albumin approached that of oxyhemoglobin, suggesting a molecular level interaction between them. The effects of serum albumin on oxyhemoglobin A were essentially similar to those on oxyhemoglobin S. Deoxy- and methemoglobins were also stabilized by serum albumin. The addition of human serum albumin to a solution containing sickle cell oxyhemoglobin slowly formed a compound which had an absorbance peak at 620 nm. After purification by Sephadex G-200 column chromatography, this compound was identified as methemalbumin. Comparison of the rates of formation of methemalbumin from hemoglobin with various ligand states and human serum albumin showed that the rate of formation from hemichrome was much faster than from met-, oxy- and deoxyhemoglobin. About 60% of the heme was transferred from hemichrome to albumin when the mixture was kept standing at room temperature for 5 min, in contrast to only 5% from methemoglobin. This result suggests that hemichrome, rather than methemoglobin, is the intermediate in the formation of methemalbumin from oxyhemoglobin and human serum albumin. This hypothesis is supported by the finding that the rate of formation of methemalbumin was faster at alkaline pH values than at acid pH values. Serum albumin from various animal sources showed different stabilizing effects. The formation of methemalbumin from these animal albumins was far less than that from human albumin. | [
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PMID:5130 | On the separation of fibrinogen degradation products D and E. | Separation of fibrinogen degradation products D and E by means of gel chromatography cannot be achieved at neutral pH even in the presence of high ionic strength of the elution buffer. It is assumed that fragments D and E are linked together in a complex preventing the separation despite different molecular weights of both components. By means of addition of chaotropic substances like 1 M Kl to the elution buffer clear separation of degradation products D and E on Sephadex G-200 columns can be achieved. | On the separation of fibrinogen degradation products D and E. Separation of fibrinogen degradation products D and E by means of gel chromatography cannot be achieved at neutral pH even in the presence of high ionic strength of the elution buffer. It is assumed that fragments D and E are linked together in a complex preventing the separation despite different molecular weights of both components. By means of addition of chaotropic substances like 1 M Kl to the elution buffer clear separation of degradation products D and E on Sephadex G-200 columns can be achieved. | [
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PMID:5131 | Affinity chromatography on hydroxyalkyl methacrylate gels. III. Adsorption of chymotrypsin to poly(hydroxyalkyl methacrylates) with covalently bound benzyloxycarbonyl-glycyl-D-phenylalanine and -D-leucine as function of pH and ionic strength. | Chymotrypsin is specifically adsorbed at low ionic strength and alkaline pH to hydroxyalkyl methacrylate gels with N-benzyloxycarbonylglycl-D-phenylalanine or N-benzyloxycarbonylglycyl-D-leucine attached through 1,6-hexanediamine. Chymotrypsin is not adsorbed either to the unmodified gel (Spheron) or to the gel with attached, 1,6-hexanediamine (NH2-Spheron). The adsorption of chymotrypsin to Z-Gly-D-Phe-NH2-Spheron was investigated as a function of pH and ionic strength. Trypsin is not adsorbed to this gel. Chymotrypsin isolated from a crude pancreatic extract by affinity chromatography on Z-Gly-D-Phe-NH2-Spheron had the same activity as the enzyme isolated on a column of Spheron, to which the naturally-occurring trypsin inhibitor had been coupled. | Affinity chromatography on hydroxyalkyl methacrylate gels. III. Adsorption of chymotrypsin to poly(hydroxyalkyl methacrylates) with covalently bound benzyloxycarbonyl-glycyl-D-phenylalanine and -D-leucine as function of pH and ionic strength. Chymotrypsin is specifically adsorbed at low ionic strength and alkaline pH to hydroxyalkyl methacrylate gels with N-benzyloxycarbonylglycl-D-phenylalanine or N-benzyloxycarbonylglycyl-D-leucine attached through 1,6-hexanediamine. Chymotrypsin is not adsorbed either to the unmodified gel (Spheron) or to the gel with attached, 1,6-hexanediamine (NH2-Spheron). The adsorption of chymotrypsin to Z-Gly-D-Phe-NH2-Spheron was investigated as a function of pH and ionic strength. Trypsin is not adsorbed to this gel. Chymotrypsin isolated from a crude pancreatic extract by affinity chromatography on Z-Gly-D-Phe-NH2-Spheron had the same activity as the enzyme isolated on a column of Spheron, to which the naturally-occurring trypsin inhibitor had been coupled. | [
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PMID:5132 | Heme-linked proton dissociation of carbon monoxide complexes of myoglobin and peroxidase. | It was found from spectrophotometric titration and proton balance measurement that the pKa value of a heme-linked protonation group of horseradish ferro-peroxidase C (donor:H2O2 oxidoreductase, EC 1.11.1.7) shifted from 7.25 to 8.25 upon combination with CO. The spectrophotometric titration experiment with myoglobin also revealed the presence of a heme-linked protonation group, the pKa value being 5.57 in myoglobin and 5.67 in the CO-myoglobin complex. It was concluded that the distinct shift of the pKa value in the case of peroxidase was attributable to the presence of a hydrogen bond between the sixth ligand and the distal base. The difference in the strength of such hydrogen bonding between peroxidase and myoglobin was discussed. | Heme-linked proton dissociation of carbon monoxide complexes of myoglobin and peroxidase. It was found from spectrophotometric titration and proton balance measurement that the pKa value of a heme-linked protonation group of horseradish ferro-peroxidase C (donor:H2O2 oxidoreductase, EC 1.11.1.7) shifted from 7.25 to 8.25 upon combination with CO. The spectrophotometric titration experiment with myoglobin also revealed the presence of a heme-linked protonation group, the pKa value being 5.57 in myoglobin and 5.67 in the CO-myoglobin complex. It was concluded that the distinct shift of the pKa value in the case of peroxidase was attributable to the presence of a hydrogen bond between the sixth ligand and the distal base. The difference in the strength of such hydrogen bonding between peroxidase and myoglobin was discussed. | [
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PMID:5133 | Isolation, characterization and partial sequence of cyanogen bromide fragments and thiol peptides from pig kidney D-amino-acid oxidase. | A partial characterization of the primary structure of D-amino-acid oxidase (D-Amino-acid:oxygen oxidoreductase (deaminating), EC 1.4.3.3.) from hog kidney has been achieved by a CNBr cleavage of the 14C-carboxymethylated protein. Four fragments have been isolated and purified and their alignment made possible by overlapping with methionine-containing peptides derived from tryptic digestion of the 14C-carboxymethylated protein. A partial sequencing of the CNBr fragments has been carried out by the automated Edman procedure and by manual sequence analysis. Chymotryptic peptides containing the 5 alkylated thiols of the monomer enzyme (Curti, B., Ronchi, S., branzoli, U., Ferri, G. and Williams, Jr., C. H. (1973) Biochim. Biophys. Acta 327, 266-273) have been isolated and their sequence determined. The present results do not show any significant homologies with the known sequences of other flavoproteins. | Isolation, characterization and partial sequence of cyanogen bromide fragments and thiol peptides from pig kidney D-amino-acid oxidase. A partial characterization of the primary structure of D-amino-acid oxidase (D-Amino-acid:oxygen oxidoreductase (deaminating), EC 1.4.3.3.) from hog kidney has been achieved by a CNBr cleavage of the 14C-carboxymethylated protein. Four fragments have been isolated and purified and their alignment made possible by overlapping with methionine-containing peptides derived from tryptic digestion of the 14C-carboxymethylated protein. A partial sequencing of the CNBr fragments has been carried out by the automated Edman procedure and by manual sequence analysis. Chymotryptic peptides containing the 5 alkylated thiols of the monomer enzyme (Curti, B., Ronchi, S., branzoli, U., Ferri, G. and Williams, Jr., C. H. (1973) Biochim. Biophys. Acta 327, 266-273) have been isolated and their sequence determined. The present results do not show any significant homologies with the known sequences of other flavoproteins. | [
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PMID:5134 | The fluorescence decay of tryptophan residues in native and denatured proteins. | The fluorescence decay kinetics at different ranges of the emission spectrum is reported for 17 proteins. Out of eight proteins containing a single tryptophan residue per molecule, seven proteins display multiexponential decay kinetics, suggesting that variability in protein structure may exist for most proteins. Tryptophan residues whose fluorescence spectrum is red shifted may have lifetimes longer than 7 ns. Such long lifetimes have not been detected in any of the denatured proteins studied, indicating that in native proteins the tryptophans having a red-shifted spectrum are affected by the tertiary structure of the protein. The fluorescence decay kinetics of ten denatured proteins studied obey multiexponential decay functions. It is therefore concluded that the tryptophan residues in denatured proteins can be grouped in two classes. The first characterized by a relatively long lifetime of about 4 ns and the second has a short lifetime of about 1.5 ns. The emission spectrum of the group which is characterized by the longer lifetime is red shifted relative to the emission spectrum of the group characterized by the shorter lifetime. A comparison of the decay data with the quantum yield of the proteins raises the possibility that a subgroup of the tryptophan residues is fully quenched. It is noteworthy that despite this heterogeneity in the environment of tryptophan residues in each denatured protein, almost the same decay kinetics has been obtained for all the denatured proteins studied in spite of the vastly different primary structures. It is therefore concluded that each tryptophan residue interacts in a more-or-less random manner with other groups on the polypeptide chain, and that on the average the different tryptophan residues in denatured proteins have a similar type of environment. | The fluorescence decay of tryptophan residues in native and denatured proteins. The fluorescence decay kinetics at different ranges of the emission spectrum is reported for 17 proteins. Out of eight proteins containing a single tryptophan residue per molecule, seven proteins display multiexponential decay kinetics, suggesting that variability in protein structure may exist for most proteins. Tryptophan residues whose fluorescence spectrum is red shifted may have lifetimes longer than 7 ns. Such long lifetimes have not been detected in any of the denatured proteins studied, indicating that in native proteins the tryptophans having a red-shifted spectrum are affected by the tertiary structure of the protein. The fluorescence decay kinetics of ten denatured proteins studied obey multiexponential decay functions. It is therefore concluded that the tryptophan residues in denatured proteins can be grouped in two classes. The first characterized by a relatively long lifetime of about 4 ns and the second has a short lifetime of about 1.5 ns. The emission spectrum of the group which is characterized by the longer lifetime is red shifted relative to the emission spectrum of the group characterized by the shorter lifetime. A comparison of the decay data with the quantum yield of the proteins raises the possibility that a subgroup of the tryptophan residues is fully quenched. It is noteworthy that despite this heterogeneity in the environment of tryptophan residues in each denatured protein, almost the same decay kinetics has been obtained for all the denatured proteins studied in spite of the vastly different primary structures. It is therefore concluded that each tryptophan residue interacts in a more-or-less random manner with other groups on the polypeptide chain, and that on the average the different tryptophan residues in denatured proteins have a similar type of environment. | [
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PMID:5135 | Endogenous proteolytic activity and constituent polypeptide chains of sheep and pig 19 S thyroglobulin. | Porcine and ovine 19-S thyroglobulins prepared from frozen glands in several buffers using slice extraction or homogenization, ammonium sulfate precipitation and DEAE-cellulose chromatography or Sepharose 6B gel filtration were contaminated with protease activity of pH optima 4.5 and 8.6, as shown by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Optimum temperatures of autodigestion were 37 degrees C at pH 4.5 and 25 degrees C at pH 8.6. Thyroglobulins prepared from unfrozen glands pH 7.2 in 0.1 M sodium phosphate using slice extraction, ammonium sulfate precipitation and Sepharose 6B gel filtration were devoid of acid proteolytic activity but still underwent autodigestion at pH 8.6. Diisopropylfluorophosphate was a potent inhibitor of the alkaline protease activity of ovine thyroglobulin preparations. In contrast to thyroglobulin obtained from frozen glands the proteins purified from fresh unfrozen glands at pH 7.2 only showed the 19-S and the 12-S species by electrophoresis in sodium dodecyl sulfate polyacrylamide gels. Very few bands migrating faster than 12-S were visible. After full reduction and S-alkylation of porcine and ovine thyroglobulins, no qualitative changes were observed in the gel electrophoresis pattern as compared to the unmodified proteins. Species of apparent mol. wt. corresponding to the native 12 S were the major component, strongly suggesting a mol. wt. of about 330 000 for the elementary peptide chains of pig and sheep thyroglobulins. | Endogenous proteolytic activity and constituent polypeptide chains of sheep and pig 19 S thyroglobulin. Porcine and ovine 19-S thyroglobulins prepared from frozen glands in several buffers using slice extraction or homogenization, ammonium sulfate precipitation and DEAE-cellulose chromatography or Sepharose 6B gel filtration were contaminated with protease activity of pH optima 4.5 and 8.6, as shown by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Optimum temperatures of autodigestion were 37 degrees C at pH 4.5 and 25 degrees C at pH 8.6. Thyroglobulins prepared from unfrozen glands pH 7.2 in 0.1 M sodium phosphate using slice extraction, ammonium sulfate precipitation and Sepharose 6B gel filtration were devoid of acid proteolytic activity but still underwent autodigestion at pH 8.6. Diisopropylfluorophosphate was a potent inhibitor of the alkaline protease activity of ovine thyroglobulin preparations. In contrast to thyroglobulin obtained from frozen glands the proteins purified from fresh unfrozen glands at pH 7.2 only showed the 19-S and the 12-S species by electrophoresis in sodium dodecyl sulfate polyacrylamide gels. Very few bands migrating faster than 12-S were visible. After full reduction and S-alkylation of porcine and ovine thyroglobulins, no qualitative changes were observed in the gel electrophoresis pattern as compared to the unmodified proteins. Species of apparent mol. wt. corresponding to the native 12 S were the major component, strongly suggesting a mol. wt. of about 330 000 for the elementary peptide chains of pig and sheep thyroglobulins. | [
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PMID:5136 | The existence of three types of acetohydroxy acid synthetase in an isoleucine-requiring mutant of Aerobacter aerogenes. | The synthesis of the three types of acetolactate synthase (EC 4.1.3.18) which are responsible for the biosynthesis os isoleucine and valine, was observed in Aerobacter aerogenes I-12, an isoleucine-requiring mutant, when grown on the four kinds of media. When the cells were grown on isoleucine-rich medium, acetolactate synthase sensitive to feedback inhibition and having an optimum pH at 8.0 was formed. By increasing the amount of potassium phosphate in the medium, the catabolite repression of the enzyme having an optimum pH at 6.0 and which is insensitive to feedback inhibition, was released. In contrast, acetolactate synthase having an optimum pH at 8.0 and insensitive to feedback inhibition was formd when isoleucine was limited, irrespective of phosphate concentrations. Two insensitive enzymes were not regulated by isoleucine, leucine and valine, although sensitive pH 8.0 enzyme was repressed by them. Thus, it may be assumed that the synthesis of insensitive pH 8.0 enzyme were repressed by limiting the amount of isoleucine is still open. | The existence of three types of acetohydroxy acid synthetase in an isoleucine-requiring mutant of Aerobacter aerogenes. The synthesis of the three types of acetolactate synthase (EC 4.1.3.18) which are responsible for the biosynthesis os isoleucine and valine, was observed in Aerobacter aerogenes I-12, an isoleucine-requiring mutant, when grown on the four kinds of media. When the cells were grown on isoleucine-rich medium, acetolactate synthase sensitive to feedback inhibition and having an optimum pH at 8.0 was formed. By increasing the amount of potassium phosphate in the medium, the catabolite repression of the enzyme having an optimum pH at 6.0 and which is insensitive to feedback inhibition, was released. In contrast, acetolactate synthase having an optimum pH at 8.0 and insensitive to feedback inhibition was formd when isoleucine was limited, irrespective of phosphate concentrations. Two insensitive enzymes were not regulated by isoleucine, leucine and valine, although sensitive pH 8.0 enzyme was repressed by them. Thus, it may be assumed that the synthesis of insensitive pH 8.0 enzyme were repressed by limiting the amount of isoleucine is still open. | [
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PMID:5137 | Identification of the chemical groups involved in the binding of periodate-oxidized NADP+ to 6-phosphogluconate dehydrogenase. | Periodate-oxidized NADP+ binds specifically and reversibly to the NADP+ binding site of 6-phosphogluconate dehydrogenase (EC 1.1.1.44) from Candida utilis. The inhibition can be stabilized by reduction with sodium borohydride. It has been shown that an aldehydic group of the inhibitor forms a Schiff base with a lysine residue of the enzyme. | Identification of the chemical groups involved in the binding of periodate-oxidized NADP+ to 6-phosphogluconate dehydrogenase. Periodate-oxidized NADP+ binds specifically and reversibly to the NADP+ binding site of 6-phosphogluconate dehydrogenase (EC 1.1.1.44) from Candida utilis. The inhibition can be stabilized by reduction with sodium borohydride. It has been shown that an aldehydic group of the inhibitor forms a Schiff base with a lysine residue of the enzyme. | [
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] |
PMID:5138 | Studies on inosine monophosphate dehydrogenase. Isotope exchange at equilibrium. | Investigations on the mechanism of the IMP dehydrogenase (IMP: NAD+ oxidoreductase, EC 1.2.1.14) reactions have been made at pH 7.0 by measuring rates of isotope exchange at chemical equilibrium with K+ maintained at a constant concentration. The results are generally in accord with the conclusions reached on the basis of the steady-state kinetic data obtained previously and confirm that there is random addition of IMP and NAD to the enzyme. The data also indicate clearly that at pH 7.0 catalysis is faster than the rate of IMP and/or XMP release which is rate limiting for the reaction sequence. The binding of IMP to the enzyme at pH 8.1 has been demonstrated to occur in the absence of both K+ and NAD and id independent of the K+ concentration. | Studies on inosine monophosphate dehydrogenase. Isotope exchange at equilibrium. Investigations on the mechanism of the IMP dehydrogenase (IMP: NAD+ oxidoreductase, EC 1.2.1.14) reactions have been made at pH 7.0 by measuring rates of isotope exchange at chemical equilibrium with K+ maintained at a constant concentration. The results are generally in accord with the conclusions reached on the basis of the steady-state kinetic data obtained previously and confirm that there is random addition of IMP and NAD to the enzyme. The data also indicate clearly that at pH 7.0 catalysis is faster than the rate of IMP and/or XMP release which is rate limiting for the reaction sequence. The binding of IMP to the enzyme at pH 8.1 has been demonstrated to occur in the absence of both K+ and NAD and id independent of the K+ concentration. | [
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PMID:5139 | Oxidation of N-methyl substituted hypoxanthines, xanthines, purine-6,8-diones and the corresponding 6-thioxo derivatives by bovine milk xanthine oxidase. | 1. The oxidation of six series of purines (hypoxanthines, xanthines, purine-6,8-diones and the corresponding 6-thioxo derivatives) by a highly purified bovine milk xanthine oxidase (EC 1.2.3.2) has been studied, using a variety of N-methyl derivatives. 2. N-Methyl substituents can either enhance or reduce enzymic rates. Enhancement is ascribed to blockade of groups which mediate unfavorable modes of binding of substrate to enzyme. Introduction of N-methyl groups can also inhibit enzymic oxidation, either by occluding essential binding groups or by preventing spontaneous or enzyme-induced tautomerisation processes, which create suitable binding sites in the substrates. 3. In all purines which are rapidly attacked by xanthine oxidase, proper attachment to the active center is mediated by the groupings (3) NH, (9) N or (3) N, (9) NH. 4. Reduced rates usually express lowered substrate affinity, which finds its expression in weak competitive inhibition of xanthine oxidation. | Oxidation of N-methyl substituted hypoxanthines, xanthines, purine-6,8-diones and the corresponding 6-thioxo derivatives by bovine milk xanthine oxidase. 1. The oxidation of six series of purines (hypoxanthines, xanthines, purine-6,8-diones and the corresponding 6-thioxo derivatives) by a highly purified bovine milk xanthine oxidase (EC 1.2.3.2) has been studied, using a variety of N-methyl derivatives. 2. N-Methyl substituents can either enhance or reduce enzymic rates. Enhancement is ascribed to blockade of groups which mediate unfavorable modes of binding of substrate to enzyme. Introduction of N-methyl groups can also inhibit enzymic oxidation, either by occluding essential binding groups or by preventing spontaneous or enzyme-induced tautomerisation processes, which create suitable binding sites in the substrates. 3. In all purines which are rapidly attacked by xanthine oxidase, proper attachment to the active center is mediated by the groupings (3) NH, (9) N or (3) N, (9) NH. 4. Reduced rates usually express lowered substrate affinity, which finds its expression in weak competitive inhibition of xanthine oxidation. | [
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PMID:5140 | Multiple forms of histone acetyltransferases in the cytosol of calf endometrium. | The histone acetyltransferase (EC 2.3.1.-) activity of calf endometrium cytosol has been separated into three separate activities by stepwise chromatography on DEAE-cellulose. In addition to differential elution from the DEAE-cellulose, the three activities are differentiated by their pH optima, preferences for histone subfractions as substrates, and stability to heat denaturation. Peak I has an optimum of pH 8.7 and preferentially acetylates histones F2b and F3; Peak II has an optimum of pH 8.5, and preferentially acetylates histone F2al followed by histone F2b; Peak III has an optimum of pH 9.5, and had similar specificity to Peak II. Peak III is appreciably more stable at 60 degrees C than is Peak II. None of the peaks transferred acetate to other proteins tested or to tRNA. These studies suggest the presence of multiple histone acetyltransferases in tissue cytosols. | Multiple forms of histone acetyltransferases in the cytosol of calf endometrium. The histone acetyltransferase (EC 2.3.1.-) activity of calf endometrium cytosol has been separated into three separate activities by stepwise chromatography on DEAE-cellulose. In addition to differential elution from the DEAE-cellulose, the three activities are differentiated by their pH optima, preferences for histone subfractions as substrates, and stability to heat denaturation. Peak I has an optimum of pH 8.7 and preferentially acetylates histones F2b and F3; Peak II has an optimum of pH 8.5, and preferentially acetylates histone F2al followed by histone F2b; Peak III has an optimum of pH 9.5, and had similar specificity to Peak II. Peak III is appreciably more stable at 60 degrees C than is Peak II. None of the peaks transferred acetate to other proteins tested or to tRNA. These studies suggest the presence of multiple histone acetyltransferases in tissue cytosols. | [
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PMID:5141 | Purification and characterization of butyrylcholine-hydrolyzing enzyme from Pseudomonas polycolor. | A butyrylcholine-hydrolyzing enzyme (EC 3.1.1.-) fo Pseudomonas polycolor IFO 3918 was purified approximately 9270-fold with a recovery of 9.9% by use of chromatographic techniques. The enzyme preparation appeared to be homogeneous when subjected to electrophoretic and ultracentrifugational analyses. The molecular weight was determined as approximately 59000 by gel filtration. Isoelectric focusing electrophoresis revealed that the enzyme had an isoelectric point around pH 5.1. The enzyme catalyzed the hydrolysis of butyrylcholine with the miximum activity among various esters tested, and split benzoylcholine, propionylcholine and some aliphatic esters, but did not attact acetylcholine. The estimated value of Km at pH 7.5 and 25 degrees C was 7-10(-4) M for butyrylcholine. The enzyme was irreversibly inhibited by organophosphorus compounds and carbamates, such as diisopropylphosphofluoridate and eserine. The enzyme was inhibited by some compounds, such as atropine and quinidine. Auaternary ammonium salts showed an inhibitory effect on the enzyme resembling co-operative inhibition. | Purification and characterization of butyrylcholine-hydrolyzing enzyme from Pseudomonas polycolor. A butyrylcholine-hydrolyzing enzyme (EC 3.1.1.-) fo Pseudomonas polycolor IFO 3918 was purified approximately 9270-fold with a recovery of 9.9% by use of chromatographic techniques. The enzyme preparation appeared to be homogeneous when subjected to electrophoretic and ultracentrifugational analyses. The molecular weight was determined as approximately 59000 by gel filtration. Isoelectric focusing electrophoresis revealed that the enzyme had an isoelectric point around pH 5.1. The enzyme catalyzed the hydrolysis of butyrylcholine with the miximum activity among various esters tested, and split benzoylcholine, propionylcholine and some aliphatic esters, but did not attact acetylcholine. The estimated value of Km at pH 7.5 and 25 degrees C was 7-10(-4) M for butyrylcholine. The enzyme was irreversibly inhibited by organophosphorus compounds and carbamates, such as diisopropylphosphofluoridate and eserine. The enzyme was inhibited by some compounds, such as atropine and quinidine. Auaternary ammonium salts showed an inhibitory effect on the enzyme resembling co-operative inhibition. | [
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PMID:5142 | A phospholipase A2 with anticoagulant activity. I. Isolation from Vipera berus venom and properties. | An anticoagulant protein has been isolated by DEAE cellulose chromatography and gel filtration from the venom of the Vipera berus orientale (Eastern Europe). Purification has been completed by elution on carboxymethyl cellulose with continuous gradient at constant pH. The inhibitor of coagulation was separated from the other venom enzymes, e.g. procoagulant, fibrinogenolytic, aminoesterase and amino acid oxidase activities. It was also separated from other phospholipase components which were not related to the anticoagulant property. The inhibitor appeared as a simgle polypeptidic chain protein, formed by 119 amino acid residues, with a molecular weight of 13400 and an isoelectric point of 9.2. At low saline molarity, a monomer-trimer transition of this protein was observed. Both forms had the same amino acid composition. There were six disulfide bridges without free SH groups per phospholipase molecule. Deprived of any proteolytic activity, the clotting inhibitor displayed a high phospholipase activity in the presence of calcium. Activity did no appear with EDTA buffer deprived of cation. Finely dispersed micellar suspensions were found suitable for obtaining the highest phospholipase activity. High sodium cholate concentration or methanol/chloroform/ether solvent were effective without loss of enzymatic activity. As characteristis of phospholipase A2 (EC 3.1.1.4), the degradation products identified on thin-layer chromatography induced hemolysis of human erythrocytes. The apparent Km value 1.25 - 10(-3) M was determined on phosphatidylcholine isolated from ovolecithin. This purified berus inhibitor would be of value for investigating the involvement of phospholipids in the clotting mechanism. | A phospholipase A2 with anticoagulant activity. I. Isolation from Vipera berus venom and properties. An anticoagulant protein has been isolated by DEAE cellulose chromatography and gel filtration from the venom of the Vipera berus orientale (Eastern Europe). Purification has been completed by elution on carboxymethyl cellulose with continuous gradient at constant pH. The inhibitor of coagulation was separated from the other venom enzymes, e.g. procoagulant, fibrinogenolytic, aminoesterase and amino acid oxidase activities. It was also separated from other phospholipase components which were not related to the anticoagulant property. The inhibitor appeared as a simgle polypeptidic chain protein, formed by 119 amino acid residues, with a molecular weight of 13400 and an isoelectric point of 9.2. At low saline molarity, a monomer-trimer transition of this protein was observed. Both forms had the same amino acid composition. There were six disulfide bridges without free SH groups per phospholipase molecule. Deprived of any proteolytic activity, the clotting inhibitor displayed a high phospholipase activity in the presence of calcium. Activity did no appear with EDTA buffer deprived of cation. Finely dispersed micellar suspensions were found suitable for obtaining the highest phospholipase activity. High sodium cholate concentration or methanol/chloroform/ether solvent were effective without loss of enzymatic activity. As characteristis of phospholipase A2 (EC 3.1.1.4), the degradation products identified on thin-layer chromatography induced hemolysis of human erythrocytes. The apparent Km value 1.25 - 10(-3) M was determined on phosphatidylcholine isolated from ovolecithin. This purified berus inhibitor would be of value for investigating the involvement of phospholipids in the clotting mechanism. | [
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PMID:5143 | A phospholipase A2 with anticoagulant activity. II. Inhibition of the phospholiped activity in coagulation. | An anticoagulant factor with phospholipase A2 activity has been isolated from Vipera berus venom. Phospholipase activity was studied on platelet phospholipid and on brain cephalin. The venom factor showed a potent anticoagulant activity: 1 mug impaired the clotting of 1 ml of citrated recalcified platelet-poor plasma. The anticoagulant inhibited clotting by antagonism to phospholipid. The antagonism constant (Kan = 6.8-10(-9) M) demonstrated the high affinity of the inhibitor for phospholipid. As with other phospholipases A2, the venom factor was thermoresistant but very sensitive to photo-oxidation. Both activities (anticoagulant activity and phospholipase activity) were not markedly dissociated by either denaturation or neutralization processes. Slightly different curves of photo-oxidative inactivation of both activities suggested the presence, on the molecule, of two very close sites responsible for phospholipase and anticoagulant activities. The inhibitor effect on coagulation was independent of the hydrolysis process. In fact, lysoderivatives and fatty acids, resulting from complete hydrolysis with the venom factor, were as active as the native phospholipids. Moreover phospholipase A2 from other viperidae venom, which did not have anticoagulant activity, produced similarly active lysoderivatives. This showed that the cleavage of the beta-acyl bond does not interfere with the activity of phospholipid. A possible mechanism of clotting inhibition by the venom factor was proposed. Owing to its high affinity for phospholipid, the inhibitor would complex phospholipid at its protein binding site impairing the normal arrangement of coagulation protein factors and, consequently, their activation. The positive charges of the inhibitor (pI = 9.2) could bind with phosphoryl or carboxyl groups of phospholipid, making them unavailable for protein binding. The complex formation involves a loss of dissociating capacity of the enzyme towards its substrate. This required an additional interaction of the inhibitor with a coagulation protein factor. The inhibitor could be removed from the complex by specific antibodies, permitting recovery of normal phospholipid-protein interaction. The role of calcium in the complex has not yet been elucidated. This venom factor affords a useful tool for investigating the phospholipid-clotting protein interaction. | A phospholipase A2 with anticoagulant activity. II. Inhibition of the phospholiped activity in coagulation. An anticoagulant factor with phospholipase A2 activity has been isolated from Vipera berus venom. Phospholipase activity was studied on platelet phospholipid and on brain cephalin. The venom factor showed a potent anticoagulant activity: 1 mug impaired the clotting of 1 ml of citrated recalcified platelet-poor plasma. The anticoagulant inhibited clotting by antagonism to phospholipid. The antagonism constant (Kan = 6.8-10(-9) M) demonstrated the high affinity of the inhibitor for phospholipid. As with other phospholipases A2, the venom factor was thermoresistant but very sensitive to photo-oxidation. Both activities (anticoagulant activity and phospholipase activity) were not markedly dissociated by either denaturation or neutralization processes. Slightly different curves of photo-oxidative inactivation of both activities suggested the presence, on the molecule, of two very close sites responsible for phospholipase and anticoagulant activities. The inhibitor effect on coagulation was independent of the hydrolysis process. In fact, lysoderivatives and fatty acids, resulting from complete hydrolysis with the venom factor, were as active as the native phospholipids. Moreover phospholipase A2 from other viperidae venom, which did not have anticoagulant activity, produced similarly active lysoderivatives. This showed that the cleavage of the beta-acyl bond does not interfere with the activity of phospholipid. A possible mechanism of clotting inhibition by the venom factor was proposed. Owing to its high affinity for phospholipid, the inhibitor would complex phospholipid at its protein binding site impairing the normal arrangement of coagulation protein factors and, consequently, their activation. The positive charges of the inhibitor (pI = 9.2) could bind with phosphoryl or carboxyl groups of phospholipid, making them unavailable for protein binding. The complex formation involves a loss of dissociating capacity of the enzyme towards its substrate. This required an additional interaction of the inhibitor with a coagulation protein factor. The inhibitor could be removed from the complex by specific antibodies, permitting recovery of normal phospholipid-protein interaction. The role of calcium in the complex has not yet been elucidated. This venom factor affords a useful tool for investigating the phospholipid-clotting protein interaction. | [
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PMID:5144 | Steady-state enzyme kinetics of the pancreatic ribonucleases from five mannalian species. | The kinetic parameters Km, k+2 and k+2/Km of the pancreatic ribonucleases (EC 3.1.4.22) from cow, giraffe, horse, rat and lesser rorqual have been determined, using 2',3'-cyclic cytidine monophosphate and 2',3'-cuclic uridine monophosphate as substrates. No large differences were found between the activities of the five enzymes. The relative differences between the activities of the five enzymes are mainly due to differences in the rates of hydrolysis and not to differences in the affinities for the substrates. | Steady-state enzyme kinetics of the pancreatic ribonucleases from five mannalian species. The kinetic parameters Km, k+2 and k+2/Km of the pancreatic ribonucleases (EC 3.1.4.22) from cow, giraffe, horse, rat and lesser rorqual have been determined, using 2',3'-cyclic cytidine monophosphate and 2',3'-cuclic uridine monophosphate as substrates. No large differences were found between the activities of the five enzymes. The relative differences between the activities of the five enzymes are mainly due to differences in the rates of hydrolysis and not to differences in the affinities for the substrates. | [
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PMID:5145 | Alpha-D-Mannosidase. Preparation and properties of free and insolubilized enzyme. | Alpha-D-Mannosidase (alpha-D-mannoside mannohydrolase, EC 3.2.1.24) has been purified to homogeneity as demonstrated by polyacrylamide gel electrophoresis and ultracentrifugation. The molecular weight of the enzyme is approx. 200000; the protein appears to contain 4 subunits, with molecular weights of 66000 and 44000. The enzyme was immobilized on Sepharose and the properties of the coupled and free enzyme were compared. Both were stable up to 70 degrees C with rapid loss of activity between 75-80 degrees C; both retained 25-30% activity in 6 M urea and 65% of the original activity could be restored in the coupled preparation by removal of the urea. The pH maximum of each form was approximately the same, with the maximum of the immobilized enzyme shifted slightly to a lower pH. The coupled alpha-D-mannosidase presented in this report offers the possibility of digesting high molecular weight substrates, such as glycoproteins, with the advantages of (1) recovering large quantities of digested substrate; (2) recovery of the active glycosidase; and (3) digestion at high temperatures and under conditions that denature many proteins. | Alpha-D-Mannosidase. Preparation and properties of free and insolubilized enzyme. Alpha-D-Mannosidase (alpha-D-mannoside mannohydrolase, EC 3.2.1.24) has been purified to homogeneity as demonstrated by polyacrylamide gel electrophoresis and ultracentrifugation. The molecular weight of the enzyme is approx. 200000; the protein appears to contain 4 subunits, with molecular weights of 66000 and 44000. The enzyme was immobilized on Sepharose and the properties of the coupled and free enzyme were compared. Both were stable up to 70 degrees C with rapid loss of activity between 75-80 degrees C; both retained 25-30% activity in 6 M urea and 65% of the original activity could be restored in the coupled preparation by removal of the urea. The pH maximum of each form was approximately the same, with the maximum of the immobilized enzyme shifted slightly to a lower pH. The coupled alpha-D-mannosidase presented in this report offers the possibility of digesting high molecular weight substrates, such as glycoproteins, with the advantages of (1) recovering large quantities of digested substrate; (2) recovery of the active glycosidase; and (3) digestion at high temperatures and under conditions that denature many proteins. | [
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PMID:5146 | Isolation and partial characterization of a protease from Agave americana variegata. | A new protease was isolated from an extract of leaves of Agave americana variegata. The protease (EC 3.4.-) was purified 565-fold with a yield of 39.5%. The 43.8 mg enzyme had a specific activity of 0.44 units/mg. According to electrophoretic, ultracentrifugal and other physical characterizations the enzyme was homogeneous. The enzyme had a MR of 57000, a S20,W-value of 4.37 S, a D20, W-value of 6.8-7.0 - 10(-7) cm2sec-1, a Stokes radius of 3.18 nm, a partial specific volume of 0.735 cm3g-1, a frictional ration of 1.25, a molecular absorbancy index at 280 nm of 5.773-10(4), an isoelectric point of 5.25 and contained 8-10% carbohydrate. The enzyme contained no cysteine. Agave protease could hydrolyze a variety of protein substrates although it did have a restricted specificity. It is not a sulphhydryl protease but seems to be an alkaline "serine" protease with an optimum pH of 7.8-8.0 Agave protease had marked esterolytic activity and with Cbz-Tyr-ONp had an apparent Michaelis constant of 0.0345 -10(-3) M and a V of 1.24 mol substrate/mol enzyme per sec. The enzyme did not need metal ions for optimal activity, monovalent cations did not influence its kinetic parameters, but it was inhibited by cobalt, pC1HgBzO- and TosPheCH2C1. With respect to its primary specificity, as well as its pH-dependence there was a resemblance with chymotrypsin, although the rate of hydrolysis of Agave protease is much lower. | Isolation and partial characterization of a protease from Agave americana variegata. A new protease was isolated from an extract of leaves of Agave americana variegata. The protease (EC 3.4.-) was purified 565-fold with a yield of 39.5%. The 43.8 mg enzyme had a specific activity of 0.44 units/mg. According to electrophoretic, ultracentrifugal and other physical characterizations the enzyme was homogeneous. The enzyme had a MR of 57000, a S20,W-value of 4.37 S, a D20, W-value of 6.8-7.0 - 10(-7) cm2sec-1, a Stokes radius of 3.18 nm, a partial specific volume of 0.735 cm3g-1, a frictional ration of 1.25, a molecular absorbancy index at 280 nm of 5.773-10(4), an isoelectric point of 5.25 and contained 8-10% carbohydrate. The enzyme contained no cysteine. Agave protease could hydrolyze a variety of protein substrates although it did have a restricted specificity. It is not a sulphhydryl protease but seems to be an alkaline "serine" protease with an optimum pH of 7.8-8.0 Agave protease had marked esterolytic activity and with Cbz-Tyr-ONp had an apparent Michaelis constant of 0.0345 -10(-3) M and a V of 1.24 mol substrate/mol enzyme per sec. The enzyme did not need metal ions for optimal activity, monovalent cations did not influence its kinetic parameters, but it was inhibited by cobalt, pC1HgBzO- and TosPheCH2C1. With respect to its primary specificity, as well as its pH-dependence there was a resemblance with chymotrypsin, although the rate of hydrolysis of Agave protease is much lower. | [
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PMID:5147 | Yeast aminopeptidase I. Chemical composition and catalytic properties. | An aminopeptidase (alpha-aminoacyl L-peptide hydrolase, EC 3.4.11.1) was purified to homogeneity from autolysates of brewer's yeast. The enzyme which is responsible for most of the yeast cell's aminopeptidase activity is a glycoprotein containing about 12% of conjugated carbohydrate and 0.02% Zn2+ and having a complex quaternary structure. The active species has a molecular weight of approx. 600000 and an isoelectric point of 4.7. The enzyme is remarkably stable, even in dilute solutions. All types of L-amino acid and peptide derivatives containing a free amino terminus are attacked, including amino acid amides and esters. As to its substrate specificity, the enzyme belongs to the so called leucine-aminopeptidases. It is strongly and specifically activated by Zn2+ and Cl- (or Br-) and inactivated by metal-chelating agents. The activation by Zn2+ seems to be mediated by a conformational transition which affects exclusively V and leads to a form of the enzyme which enhanced stability against heat. Halide anions, on the other hand, are acting as positive allosteric effectors, modulating both V and Km. | Yeast aminopeptidase I. Chemical composition and catalytic properties. An aminopeptidase (alpha-aminoacyl L-peptide hydrolase, EC 3.4.11.1) was purified to homogeneity from autolysates of brewer's yeast. The enzyme which is responsible for most of the yeast cell's aminopeptidase activity is a glycoprotein containing about 12% of conjugated carbohydrate and 0.02% Zn2+ and having a complex quaternary structure. The active species has a molecular weight of approx. 600000 and an isoelectric point of 4.7. The enzyme is remarkably stable, even in dilute solutions. All types of L-amino acid and peptide derivatives containing a free amino terminus are attacked, including amino acid amides and esters. As to its substrate specificity, the enzyme belongs to the so called leucine-aminopeptidases. It is strongly and specifically activated by Zn2+ and Cl- (or Br-) and inactivated by metal-chelating agents. The activation by Zn2+ seems to be mediated by a conformational transition which affects exclusively V and leads to a form of the enzyme which enhanced stability against heat. Halide anions, on the other hand, are acting as positive allosteric effectors, modulating both V and Km. | [
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PMID:5148 | Preparation and enzymatic properties of subtilisin Novo chemically attached to soluble DEAE-dextran and insoluble DEAE-sephadex. | Analogous soluble and insoluble derivatives of subtilisin Novo (EC 3.4.21.14) were prepared by coupling the enzyme to CNBr-activated DEAE-dextran and DEAE-Sephadex, respectively. The DEAE-dextran-subtilisin displayed pH optima and Km values for ester hydrolysis similar to subtilisin, whereas the pH versus activity profiles obtained with DEAE-Sephadex-subtilisin were shifter towards the alkaline pH region and the Km values were increased. Compared with subtilisin, DEAE-dextran-subtilisin showed a 40-65% reduction of kcat for hydrolysis of N-acetyl-L-tyrosine ethyl ester, p-tosyl-L-arginine methyl ester and benzyloxycarbonyl-glycyl-L-tyrosinamide and its maximum velocities for digestion of casein and clupein also amounted to 40-60% of the subtilisin values. With Deae-sephadex-subtilisin, in contrast, the maximum velocity of hydrolysis decreased to a greater extent for polypeptide substrates compared to ester substrates. The present results indicate that the chemical nature of a support can effect intrinsic properties of a matrix-bound enzyme in addition to the steric and diffusional effects usually observed with polymer-attached enzymes. | Preparation and enzymatic properties of subtilisin Novo chemically attached to soluble DEAE-dextran and insoluble DEAE-sephadex. Analogous soluble and insoluble derivatives of subtilisin Novo (EC 3.4.21.14) were prepared by coupling the enzyme to CNBr-activated DEAE-dextran and DEAE-Sephadex, respectively. The DEAE-dextran-subtilisin displayed pH optima and Km values for ester hydrolysis similar to subtilisin, whereas the pH versus activity profiles obtained with DEAE-Sephadex-subtilisin were shifter towards the alkaline pH region and the Km values were increased. Compared with subtilisin, DEAE-dextran-subtilisin showed a 40-65% reduction of kcat for hydrolysis of N-acetyl-L-tyrosine ethyl ester, p-tosyl-L-arginine methyl ester and benzyloxycarbonyl-glycyl-L-tyrosinamide and its maximum velocities for digestion of casein and clupein also amounted to 40-60% of the subtilisin values. With Deae-sephadex-subtilisin, in contrast, the maximum velocity of hydrolysis decreased to a greater extent for polypeptide substrates compared to ester substrates. The present results indicate that the chemical nature of a support can effect intrinsic properties of a matrix-bound enzyme in addition to the steric and diffusional effects usually observed with polymer-attached enzymes. | [
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PMID:5149 | Photocontrol of urease-collagen membrane activity. | (1) Urease (EC 3.5.1.5.) was modified with beta-1-[3,3-dimethyl-6'-nitrospiro-(indoline-2,2'-2H-benzopyrene)] propionic anhydride. Three amino acid residues of urease were modified by the anhydride at a molar ratio of 2000. (2) The activity of modified urease was decreased with ultraviolet irradiation and then restored to the initial activity with visible light irradiation. (3) Modified urease was used to prepare a urease-collagen membrane. The apparent Michaelis constant (Km) of the modified urease-collagen membrane ultraviolet light was identical to that of the membrane under visible light. (4) The optimum pH of the modified urease-collagen membrane was displaced toward lower pH values with ultraviolet irradiation. At higher ionic strength, the pH activity curve of the membrane was displaced toward higher pH values. (5) The thermostability of urease was increased with its modification. | Photocontrol of urease-collagen membrane activity. (1) Urease (EC 3.5.1.5.) was modified with beta-1-[3,3-dimethyl-6'-nitrospiro-(indoline-2,2'-2H-benzopyrene)] propionic anhydride. Three amino acid residues of urease were modified by the anhydride at a molar ratio of 2000. (2) The activity of modified urease was decreased with ultraviolet irradiation and then restored to the initial activity with visible light irradiation. (3) Modified urease was used to prepare a urease-collagen membrane. The apparent Michaelis constant (Km) of the modified urease-collagen membrane ultraviolet light was identical to that of the membrane under visible light. (4) The optimum pH of the modified urease-collagen membrane was displaced toward lower pH values with ultraviolet irradiation. At higher ionic strength, the pH activity curve of the membrane was displaced toward higher pH values. (5) The thermostability of urease was increased with its modification. | [
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PMID:5150 | Fluoride inhibition of inorganic pyrophosphatase. I. Kinetic studies in a Mg2+-PPi system using a new continuous enzyme assay. | Reversible inhibition of bakers' yeast inorganic pyrophosphatase (EC 3.6.1.1) by fluoride has been studied as a function of substrate, metal-ion activator and inhibitor concentrations and pH using a new continuous enzyme assay with an automatic phosphate analyzer. The inhibition was shown to be the result of tight binding of fluoride by two catalytically active enzyme-substrate complexes. The reaction between pyrophosphatase and fluoride is relatively slow, so that the rate constants for the binding and release of the inhibitor were derived from phosphate formation curves measured on the time scale of enzyme assays. The pH-dependence of the inhibition reaction in the alkaline medium indicates that both the fluoride-enzyme interaction and the catalytic step of the pyrophosphatase reaction are controlled by the same group on the protein. In the acidic medium, the inhibition is considerably enhanced, presumably because of the protonation of another enzyme group. | Fluoride inhibition of inorganic pyrophosphatase. I. Kinetic studies in a Mg2+-PPi system using a new continuous enzyme assay. Reversible inhibition of bakers' yeast inorganic pyrophosphatase (EC 3.6.1.1) by fluoride has been studied as a function of substrate, metal-ion activator and inhibitor concentrations and pH using a new continuous enzyme assay with an automatic phosphate analyzer. The inhibition was shown to be the result of tight binding of fluoride by two catalytically active enzyme-substrate complexes. The reaction between pyrophosphatase and fluoride is relatively slow, so that the rate constants for the binding and release of the inhibitor were derived from phosphate formation curves measured on the time scale of enzyme assays. The pH-dependence of the inhibition reaction in the alkaline medium indicates that both the fluoride-enzyme interaction and the catalytic step of the pyrophosphatase reaction are controlled by the same group on the protein. In the acidic medium, the inhibition is considerably enhanced, presumably because of the protonation of another enzyme group. | [
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PMID:5151 | Hydrolysis of neutral glycerides by lipases of rat brain microsomes. | The hydrolysis of monoacylglycerol and diacylglycerol by rat brain microsomes was followed by measuring the release of glycerol and monooleylglycerol from dispersions of water insoluble glyceryl esters of oleic acid. The microsomes showed three lipolytic activities. One activity, optimal at pH 4.8, catalyzed the hydrolysis of diacylglycerol but not monoacylglycerol. Two other lipolytic activities, optimal at pH 8.0-8.6, catalyzed the hydrolysis of both diacylglycerol and monoacylglycerol. The pH 8.0-8.6 activities were sensitive to heat and SH-reagents. Detergents were inhibitory in all cases. Extraction of the microsomes with KCl, KSCN, urea or Triton X-100 did not change the ratio of diacylglycerol hydrolysis at pH 4.8 and 8.0. The results of subcellular fractionation studies showed that there was no significant enrichment of the acid lipase in any fraction. | Hydrolysis of neutral glycerides by lipases of rat brain microsomes. The hydrolysis of monoacylglycerol and diacylglycerol by rat brain microsomes was followed by measuring the release of glycerol and monooleylglycerol from dispersions of water insoluble glyceryl esters of oleic acid. The microsomes showed three lipolytic activities. One activity, optimal at pH 4.8, catalyzed the hydrolysis of diacylglycerol but not monoacylglycerol. Two other lipolytic activities, optimal at pH 8.0-8.6, catalyzed the hydrolysis of both diacylglycerol and monoacylglycerol. The pH 8.0-8.6 activities were sensitive to heat and SH-reagents. Detergents were inhibitory in all cases. Extraction of the microsomes with KCl, KSCN, urea or Triton X-100 did not change the ratio of diacylglycerol hydrolysis at pH 4.8 and 8.0. The results of subcellular fractionation studies showed that there was no significant enrichment of the acid lipase in any fraction. | [
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PMID:5153 | The effect of soluble rat liver proteins on the activity of microsomal stearoyl-CoA and linoleoyl-CoA desaturase. | 1. The influence of bovine serum albumin and soluble rat liver proteins on the activity of rat liver microsomal delta9 and delta6 desaturases has been studied. 2. In the absence of bovine serum albumin, the delta9 desaturase which converts stearoyl-CoA into oleoyl-CoA, shows a non-linear correlation between enzyme activity and protein concentration. 3. Optimum concentrations of bovine serum albumin have three main effects on the enzyme activity: (i) establishes a linear relationship between enzyme activity and protein concentration, (ii) stimulates the enzyme activity 2--3-fold and (iii) raises the optimum substrate concentration from 10 to 100 muM. 4. A highly purified soluble liver protein of molecular weight 24 000 also stimulated the enzyme activity and brought about a linear relationship between enzyme activity and protein concentration. 5. It was concluded that the non-linear kinetics were due to limiting amounts of substrate binding protein in the microsomal preparations. 6. The delta6 desaturase which converts linoleoyl-CoA into gamma-linolenoyl-CoA was also stimulated by bovine serum albumin and soluble liver proteins. 7. The significance of the fatty acid-binding proteins is discussed. | The effect of soluble rat liver proteins on the activity of microsomal stearoyl-CoA and linoleoyl-CoA desaturase. 1. The influence of bovine serum albumin and soluble rat liver proteins on the activity of rat liver microsomal delta9 and delta6 desaturases has been studied. 2. In the absence of bovine serum albumin, the delta9 desaturase which converts stearoyl-CoA into oleoyl-CoA, shows a non-linear correlation between enzyme activity and protein concentration. 3. Optimum concentrations of bovine serum albumin have three main effects on the enzyme activity: (i) establishes a linear relationship between enzyme activity and protein concentration, (ii) stimulates the enzyme activity 2--3-fold and (iii) raises the optimum substrate concentration from 10 to 100 muM. 4. A highly purified soluble liver protein of molecular weight 24 000 also stimulated the enzyme activity and brought about a linear relationship between enzyme activity and protein concentration. 5. It was concluded that the non-linear kinetics were due to limiting amounts of substrate binding protein in the microsomal preparations. 6. The delta6 desaturase which converts linoleoyl-CoA into gamma-linolenoyl-CoA was also stimulated by bovine serum albumin and soluble liver proteins. 7. The significance of the fatty acid-binding proteins is discussed. | [
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PMID:5154 | Control of the formation of extracellular ribonuclease in Neurospora crassa. | A finding was made that a species of ribonuclease is released into mycelial culture media when a wild-type strain of Neurospora crassa was grown on limiting amounts of phosphate. The ribonuclease activity in the fully derepressed state extends to about 60 to 100 fold of that in the repressed state. The synthesis of the ribonuclease was inhibited by the addition of rifampicin, cycloheximide or orthophosphate. Three molecular species of the ribonuclease were found. Two enzyme fractions showing larger molecular weights were suspected to be aggregates containing the enzyme showing the smallest molecular weight (molecular weight of 10 300). All three fractions showed pH optima of around 7, preferential hydrolysis of polyguanylic acid and poor hydrolysis of guanosine 2',3',-cyclic monophosphate. These characteristics were the same as those of ribonuclease N1, and it was suggested that ribonuclease N1 is a repressible extracellular enzyme. Mutations in the genes nuc-1 and nuc-2 caused loss of ability to derepress this enzyme, but heterokaryon between them partially restored the ability. The nuc-1 mutation was epistatic to the nuc-2 alleles which are partly constitutive in the ribonuclease production. | Control of the formation of extracellular ribonuclease in Neurospora crassa. A finding was made that a species of ribonuclease is released into mycelial culture media when a wild-type strain of Neurospora crassa was grown on limiting amounts of phosphate. The ribonuclease activity in the fully derepressed state extends to about 60 to 100 fold of that in the repressed state. The synthesis of the ribonuclease was inhibited by the addition of rifampicin, cycloheximide or orthophosphate. Three molecular species of the ribonuclease were found. Two enzyme fractions showing larger molecular weights were suspected to be aggregates containing the enzyme showing the smallest molecular weight (molecular weight of 10 300). All three fractions showed pH optima of around 7, preferential hydrolysis of polyguanylic acid and poor hydrolysis of guanosine 2',3',-cyclic monophosphate. These characteristics were the same as those of ribonuclease N1, and it was suggested that ribonuclease N1 is a repressible extracellular enzyme. Mutations in the genes nuc-1 and nuc-2 caused loss of ability to derepress this enzyme, but heterokaryon between them partially restored the ability. The nuc-1 mutation was epistatic to the nuc-2 alleles which are partly constitutive in the ribonuclease production. | [
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PMID:5156 | Magnetic and spectroscopic probes for FeOFe linkages in hemin systems. | Magnetic and spectroscopic properties of mu-oxo-bis-hemins from natural and structurally related porphyrins were investigated as probes for ascertaining the presence or absence of FeIII-O-FeIII linkages between hemin moieties of hemeproteins. Magnetic susceptibilities of solids from 2.2 to 293 degrees K were investigated. The data fit the temperature variations expected for a pair of antiferromagnetically coupled S = 5/2, iron (III) porphyrins with J values of 175, 190, 195, 205, and 210 degrees K for deuterohemins with hydrogen, vinyl, 2'-ethoxycarbonylcyclopropyl, acetyl, propionyl, and ethyl 2,4-substituents, respectively. This magnetic character is reflected in PMR spectra that exhibit resonances with far less broadening and paramagnetic shift than is the case for monomeric high-spin hemins. Only impurities are seen in EPR spectra, which serve effectively in monitoring the magnetic purity of preparations. An infrared active asymmetric stretching frequency characteristic of the FeOFe linkage can be identified by substitution of 160 by 180. Electronic spectra are highly characteristic with poorly resolved absorption bands. The substituents on the porphyrin ring exert significant, but usually not large, electronic and steric effects on these properties. Solvent effects were relatively small and no firm evidence for binding of ligands trans to bridging oxygen was found. The uniqueness of these physical properties and their low sensitivity to changes in porphyrin structure or medium facilitates the identification of mu-oxo linkage in hemins or oxidized hemeproteins. | Magnetic and spectroscopic probes for FeOFe linkages in hemin systems. Magnetic and spectroscopic properties of mu-oxo-bis-hemins from natural and structurally related porphyrins were investigated as probes for ascertaining the presence or absence of FeIII-O-FeIII linkages between hemin moieties of hemeproteins. Magnetic susceptibilities of solids from 2.2 to 293 degrees K were investigated. The data fit the temperature variations expected for a pair of antiferromagnetically coupled S = 5/2, iron (III) porphyrins with J values of 175, 190, 195, 205, and 210 degrees K for deuterohemins with hydrogen, vinyl, 2'-ethoxycarbonylcyclopropyl, acetyl, propionyl, and ethyl 2,4-substituents, respectively. This magnetic character is reflected in PMR spectra that exhibit resonances with far less broadening and paramagnetic shift than is the case for monomeric high-spin hemins. Only impurities are seen in EPR spectra, which serve effectively in monitoring the magnetic purity of preparations. An infrared active asymmetric stretching frequency characteristic of the FeOFe linkage can be identified by substitution of 160 by 180. Electronic spectra are highly characteristic with poorly resolved absorption bands. The substituents on the porphyrin ring exert significant, but usually not large, electronic and steric effects on these properties. Solvent effects were relatively small and no firm evidence for binding of ligands trans to bridging oxygen was found. The uniqueness of these physical properties and their low sensitivity to changes in porphyrin structure or medium facilitates the identification of mu-oxo linkage in hemins or oxidized hemeproteins. | [
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PMID:5157 | Copper (II) induced polymerization of human albumin, and its depolymerization by diglycyl-L-histidine: a pH static and ultracentrifugation study. | Copper (II) ions successively induce dimers and tetramers of human serum albumin (L) when the Cu (II) concentration is extended beyond that of 200 muM. This is shown by emf titrations and by ultracentrifugation experiments. The emf titrations, which involve a new pH static method, were performed at 25 degrees, in a 0.5 M NaCIO4 medium at pH 6.59, using glass and copper amalgam electrodes. The total concentration of Cu(II) varied from 0.14 to 2.2 mM and the albumin concentration from 0.05 to 0.7 mM. In order to evaluate the formula of the main complexes, without using any a priori assumptions regarding their compositions, a detailed graphic procedure was used. The results, in the form of equilibrium constants for the main species, were refined by the use of a general least squares computer program. The experimental data are found to be consistent with the formation of the monomeric CuL, Cu5L, and Cu6L species and the dimeric Cu3L2, Cu4L, Cu6L, and Cu8L2 species. In addition, there is some indication for a minor species, most probably the Cu12L4 tetramer. The pH static results qualitatively agree with the findings obtained by ultracentrifugation. As indicated by distinct bands and their S-values, ultracentrifugation experiments show not only monomeric and dimeric species of albumin, but also tetrameric species. The polymerization of the albumin is reversible, since diglycyl-L-histidine, a peptide designed to mimic the Cu (II) transport site of albumin, depolymerizes the Cu (II)-albumin polymers. | Copper (II) induced polymerization of human albumin, and its depolymerization by diglycyl-L-histidine: a pH static and ultracentrifugation study. Copper (II) ions successively induce dimers and tetramers of human serum albumin (L) when the Cu (II) concentration is extended beyond that of 200 muM. This is shown by emf titrations and by ultracentrifugation experiments. The emf titrations, which involve a new pH static method, were performed at 25 degrees, in a 0.5 M NaCIO4 medium at pH 6.59, using glass and copper amalgam electrodes. The total concentration of Cu(II) varied from 0.14 to 2.2 mM and the albumin concentration from 0.05 to 0.7 mM. In order to evaluate the formula of the main complexes, without using any a priori assumptions regarding their compositions, a detailed graphic procedure was used. The results, in the form of equilibrium constants for the main species, were refined by the use of a general least squares computer program. The experimental data are found to be consistent with the formation of the monomeric CuL, Cu5L, and Cu6L species and the dimeric Cu3L2, Cu4L, Cu6L, and Cu8L2 species. In addition, there is some indication for a minor species, most probably the Cu12L4 tetramer. The pH static results qualitatively agree with the findings obtained by ultracentrifugation. As indicated by distinct bands and their S-values, ultracentrifugation experiments show not only monomeric and dimeric species of albumin, but also tetrameric species. The polymerization of the albumin is reversible, since diglycyl-L-histidine, a peptide designed to mimic the Cu (II) transport site of albumin, depolymerizes the Cu (II)-albumin polymers. | [
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PMID:5158 | Studies on Copper-Acetylglycylglycine System. | Reported here are studies on the copper-acetylgylcylglycine system as a function of pH and the molar ratio between the ligand and the paramagnetic ion, applying potentiometric titration, magnetic resonances (esr and nmr) and spectrophotometric techniques. The results indicate that depending on the pH of the solutions there are three distinct regions characterized by their different species and behavior. In region I (pH less than 6.5), the copper is bound to the carboxylate group of the ligand molecule (the "blue" complex). Precipitation of copper occurs in region II (pH-7). In region III (pH greater than 9), in the presence of excess of ligand, the copper redissolves, forming complexes in which the central copper ion binds to the peptide molecule, through the nitrogens of the deprotonated peptide groups, and to hydroxyl ions. The mutual replacement of the peptide groups of chelated AcGlyGly by OH- and the changes in the structures of the complexes are discussed. | Studies on Copper-Acetylglycylglycine System. Reported here are studies on the copper-acetylgylcylglycine system as a function of pH and the molar ratio between the ligand and the paramagnetic ion, applying potentiometric titration, magnetic resonances (esr and nmr) and spectrophotometric techniques. The results indicate that depending on the pH of the solutions there are three distinct regions characterized by their different species and behavior. In region I (pH less than 6.5), the copper is bound to the carboxylate group of the ligand molecule (the "blue" complex). Precipitation of copper occurs in region II (pH-7). In region III (pH greater than 9), in the presence of excess of ligand, the copper redissolves, forming complexes in which the central copper ion binds to the peptide molecule, through the nitrogens of the deprotonated peptide groups, and to hydroxyl ions. The mutual replacement of the peptide groups of chelated AcGlyGly by OH- and the changes in the structures of the complexes are discussed. | [
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PMID:5155 | [Effect of pH on the separation of rat liver cells]. | The effect of calcium ions, temperature and pH on the number of cells separated in the course of dispersion procedure was studied. The maximum number of separated cells corresponds to pH 6.8. Mechanical resistibility of the cells in suspension was found to grow linearly within pH interval 5.2-8.8. | [Effect of pH on the separation of rat liver cells]. The effect of calcium ions, temperature and pH on the number of cells separated in the course of dispersion procedure was studied. The maximum number of separated cells corresponds to pH 6.8. Mechanical resistibility of the cells in suspension was found to grow linearly within pH interval 5.2-8.8. | [
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PMID:5162 | A method for the estimation of acetanilide, paracetamol and phenacetin in plasma and urine using mass fragmentography. | Phenacetin, paracetamol and acetanilide can be determined in a plasma or urine sample by the use of deuterium labelled analogues. These are produced by reaction of hexadeuterioacetic anhydride with the appropriate aromatic amine. The -NHCOCD3 group is stable to hydrogen exchange below pH 8. The internal standard is added to the plasma or urine after enzymatic hydrolysis of the paracetamol conjugates and an ethyl acetate extract at pH 5 is evaporated under nitrogen and the residue derivatized with N,O-bis-(trimethylsilyl)-acetamide. An aliquot of this solution is injected into a g.c.m.s. system, and one ion characteristic of the material under study and the ion from the deuterium analogue (3 mass units greater) are monitored using a voltage switching technique. In the case of phenacetin, for example, ions at 251 and 254 are monitored. Calibration curves relating different weight ratios of the hydrogen and deuterium compounds to their respective signals from the gas chromatography mass spectrometer are used to calculate the amount of a compound in a particular sample. These methods have been developed to study the oxidation of acetanilide to paracetamol and the de-ethylation of phenacetin to paracetamol. Preliminary results from experiments with phenacetin will be discussed. | A method for the estimation of acetanilide, paracetamol and phenacetin in plasma and urine using mass fragmentography. Phenacetin, paracetamol and acetanilide can be determined in a plasma or urine sample by the use of deuterium labelled analogues. These are produced by reaction of hexadeuterioacetic anhydride with the appropriate aromatic amine. The -NHCOCD3 group is stable to hydrogen exchange below pH 8. The internal standard is added to the plasma or urine after enzymatic hydrolysis of the paracetamol conjugates and an ethyl acetate extract at pH 5 is evaporated under nitrogen and the residue derivatized with N,O-bis-(trimethylsilyl)-acetamide. An aliquot of this solution is injected into a g.c.m.s. system, and one ion characteristic of the material under study and the ion from the deuterium analogue (3 mass units greater) are monitored using a voltage switching technique. In the case of phenacetin, for example, ions at 251 and 254 are monitored. Calibration curves relating different weight ratios of the hydrogen and deuterium compounds to their respective signals from the gas chromatography mass spectrometer are used to calculate the amount of a compound in a particular sample. These methods have been developed to study the oxidation of acetanilide to paracetamol and the de-ethylation of phenacetin to paracetamol. Preliminary results from experiments with phenacetin will be discussed. | [
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PMID:5168 | Studies on the chemical nature of urinary chemiluminescence. | Studies on the nature of the chemicals responsible for urinary chemiluminescence have been carried out. Urinary chemiluminescence can be increased slightly by sulphatase, more by glucuronidase but most of all by boiling for 1 hour at pH 1. It is suggested that most of the chemicals responsible for urinary chemiluminescence are bound as non-chemiluminescent precursors to sulphate, glucuronic acid and in other ways. Both the chemiluminescent material and the inactive precursors are freely ultrafiltrable with molecular weights below 500. A survey of various chemicals has revealed considerable chemiluminescence in certain metabolites of naphthylamines and known to cause bladder cancer but little or no chemoluminescence in the tryptophane metabolites that have been thought to cause bladder cancer. | Studies on the chemical nature of urinary chemiluminescence. Studies on the nature of the chemicals responsible for urinary chemiluminescence have been carried out. Urinary chemiluminescence can be increased slightly by sulphatase, more by glucuronidase but most of all by boiling for 1 hour at pH 1. It is suggested that most of the chemicals responsible for urinary chemiluminescence are bound as non-chemiluminescent precursors to sulphate, glucuronic acid and in other ways. Both the chemiluminescent material and the inactive precursors are freely ultrafiltrable with molecular weights below 500. A survey of various chemicals has revealed considerable chemiluminescence in certain metabolites of naphthylamines and known to cause bladder cancer but little or no chemoluminescence in the tryptophane metabolites that have been thought to cause bladder cancer. | [
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PMID:5174 | Role of the practitioner, public health officer, dermatologist, and other specialists in the teaching, investigation and treatment of STD. The situation in the Common Market countries. | The training of undergraduates and postgraduates in the original member countries of the European Community (Belgium, Federal Republic of Germany, France, Italy, Luxemburg, and the Netherlands) is outlined and compared with training in the U.K. and Ireland. It is noted that, in the European Community, training is inadequate and should be improved. Harmonizing with the U.K. will require concessions to be made on both sides. | Role of the practitioner, public health officer, dermatologist, and other specialists in the teaching, investigation and treatment of STD. The situation in the Common Market countries. The training of undergraduates and postgraduates in the original member countries of the European Community (Belgium, Federal Republic of Germany, France, Italy, Luxemburg, and the Netherlands) is outlined and compared with training in the U.K. and Ireland. It is noted that, in the European Community, training is inadequate and should be improved. Harmonizing with the U.K. will require concessions to be made on both sides. | [
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PMID:5175 | Effects of axotomy on the trans-synaptic regulation of enzyme activity in adult rat superior cervical ganglia. | The effects of surgical transection of the postganglionic nerve trunk of the superior cervical ganglion on the total protein content and levels of the enzymes tyrosine hydroxylase, DOPA decarboxylase and choline acetyltransferase have been studied in the adult rat. There is a minor decrease in the total activities of these 3 enzymes accompanied by a large increase in the total protein content of the ganglion. The trans-synaptic induction of the enzyme tyrosine hydroxylase by reserpine is not affected by postganglionic axotomy. Increased activity mediated by reserpine caused no change in the total activities of either DOPA decarboxylase or choline acetyltransferase. Previously observed effects of postganglionic axotomy on preventing transmission through the ganglion are compared with these results and the possible mechanisms by which trans-synaptic induction may occur are discussed. | Effects of axotomy on the trans-synaptic regulation of enzyme activity in adult rat superior cervical ganglia. The effects of surgical transection of the postganglionic nerve trunk of the superior cervical ganglion on the total protein content and levels of the enzymes tyrosine hydroxylase, DOPA decarboxylase and choline acetyltransferase have been studied in the adult rat. There is a minor decrease in the total activities of these 3 enzymes accompanied by a large increase in the total protein content of the ganglion. The trans-synaptic induction of the enzyme tyrosine hydroxylase by reserpine is not affected by postganglionic axotomy. Increased activity mediated by reserpine caused no change in the total activities of either DOPA decarboxylase or choline acetyltransferase. Previously observed effects of postganglionic axotomy on preventing transmission through the ganglion are compared with these results and the possible mechanisms by which trans-synaptic induction may occur are discussed. | [
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PMID:5176 | The effects of putative neurotransmitters on the resting membrane potential of dissociated brain neurones in culture. | Cultures established from mechanically dissociated neonatal mouse brains were found to be suitable for electrophysiological investigation of drug action. During culture most cells were aggregated into either monolayer regions or thick cords joining monolayer regions. A few cells remained isolated. The neurones in the monolayer regions were distinguished from glial cells by differential staining, and were found to be the best subject for intracellular recording. Frequency of resting membrane potentials of these cells proved to be reproducible in cultures of the same age, and were a useful index of sensitivity to bath applied drugs. Acetylcholine, dopamine, histamine, serotonin and noradrenaline depolarized various neurones; GABA caused hyperpolarization, while glutamate and glycine had no significant effect. Antagonism of the responses to acetylcholine, dopamine, serotonin and GABA was seen using atropine, pimozide, methysergide and bicuculline respectively. It is concluded that dissociated brain neurones in culture show chemosensitivity and may be useful in further pharmacological studies. | The effects of putative neurotransmitters on the resting membrane potential of dissociated brain neurones in culture. Cultures established from mechanically dissociated neonatal mouse brains were found to be suitable for electrophysiological investigation of drug action. During culture most cells were aggregated into either monolayer regions or thick cords joining monolayer regions. A few cells remained isolated. The neurones in the monolayer regions were distinguished from glial cells by differential staining, and were found to be the best subject for intracellular recording. Frequency of resting membrane potentials of these cells proved to be reproducible in cultures of the same age, and were a useful index of sensitivity to bath applied drugs. Acetylcholine, dopamine, histamine, serotonin and noradrenaline depolarized various neurones; GABA caused hyperpolarization, while glutamate and glycine had no significant effect. Antagonism of the responses to acetylcholine, dopamine, serotonin and GABA was seen using atropine, pimozide, methysergide and bicuculline respectively. It is concluded that dissociated brain neurones in culture show chemosensitivity and may be useful in further pharmacological studies. | [
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