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PMID:12750 | Effect of phenylalanine metabolites on the activities of enzymes of ketone-body utilization in brain of suckling rats. | 1. The effects of phenylalanine and its metabolites (phenylacetate, phenethylamine, phenyl-lactate, o-hydroxyphenylacetate and phenylpyruvate) on the activity of 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) 3-oxo acid CoA-transferase (EC 2.8.3.5) and acetoacetyl-CoA thiolase (EC 2.3.1.9) in brain of suckling rats were investigated. 2. The 3-hydroxybutyrate dehydrogenase from the brain of suckling rats had a Km for 3-hydroxybutyrate of 1.2 mM. Phenylpyruvate, phenylacetate and o-hydroxyphenylacetate inhibited the enzyme activity with Ki values of 0.5, 1.3 and 4.7 mM respectively. 3. The suckling-rat brain 3-oxo acid CoA-transferase activity had a Km for acetoacetate of 0.665 mM and for succinyl (3-carboxypropionyl)-CoA of 0.038 mM. The enzyme was inhibited with respect to acetoacetate by phenylpyruvate (Ki equals 1.3 mM) and o-hydroxyphenylacetate (Ki equals 4.5 mM). The reaction in the direction of acetoacetate was also inhibited by phenylpyruvate (Ki equals 1.6 mM) and o-hydroxyphenylacetate (Ki equals 4.5 mM). 4. Phenylpyruvate inhibited with respect to acetoacetyl-CoA both the mitochondrial (Ki equals 3.2 mM) and cytoplasmic (Ki equals 5.2 mM) acetoacetyl-CoA thiolase activities. 5. The results suggest that inhibition of 3-hydroxybutyrate dehydrogenase and 3-oxo acid CoA-transferase activities may impair ketone-body utilization and hence lipid synthesis in the developing brain. This suggestion is discussed with reference to the pathogenesis of mental retardation in phenylketonuria. | Effect of phenylalanine metabolites on the activities of enzymes of ketone-body utilization in brain of suckling rats. 1. The effects of phenylalanine and its metabolites (phenylacetate, phenethylamine, phenyl-lactate, o-hydroxyphenylacetate and phenylpyruvate) on the activity of 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) 3-oxo acid CoA-transferase (EC 2.8.3.5) and acetoacetyl-CoA thiolase (EC 2.3.1.9) in brain of suckling rats were investigated. 2. The 3-hydroxybutyrate dehydrogenase from the brain of suckling rats had a Km for 3-hydroxybutyrate of 1.2 mM. Phenylpyruvate, phenylacetate and o-hydroxyphenylacetate inhibited the enzyme activity with Ki values of 0.5, 1.3 and 4.7 mM respectively. 3. The suckling-rat brain 3-oxo acid CoA-transferase activity had a Km for acetoacetate of 0.665 mM and for succinyl (3-carboxypropionyl)-CoA of 0.038 mM. The enzyme was inhibited with respect to acetoacetate by phenylpyruvate (Ki equals 1.3 mM) and o-hydroxyphenylacetate (Ki equals 4.5 mM). The reaction in the direction of acetoacetate was also inhibited by phenylpyruvate (Ki equals 1.6 mM) and o-hydroxyphenylacetate (Ki equals 4.5 mM). 4. Phenylpyruvate inhibited with respect to acetoacetyl-CoA both the mitochondrial (Ki equals 3.2 mM) and cytoplasmic (Ki equals 5.2 mM) acetoacetyl-CoA thiolase activities. 5. The results suggest that inhibition of 3-hydroxybutyrate dehydrogenase and 3-oxo acid CoA-transferase activities may impair ketone-body utilization and hence lipid synthesis in the developing brain. This suggestion is discussed with reference to the pathogenesis of mental retardation in phenylketonuria. | [
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PMID:12751 | Nicotinamide-adenine dinucleotide-linked "malic" enzyme in flight muscle of the tse-tse fly (Glossina) and other insects. | 1. A high activity of NAD-linked "malic" enzyme was found in homogenates of flight muscle of different species of tse-tse fly (Glossina). The activity was the same as, or higher than, that of malate dehydrogenase and more than 20-fold that of NADP-linked "malic" enzyme. A similar enzyme was found in the flight muscle of all other insects investigated, but at much lower activities. 2. ACa2+-stimulated oxaloacetate decarboxylase activity was present in all insect flight-muscle preparations investigated, in constant proportion to the NAD-linked "malic" enzyme. 3. A partial purification of the NAD-linked "malic" enzyme from Glossina was effected by DEAE-cellulose chromatography, which separated the enzyme from malate dehydrogenase and NADP-linked "malic" enzyme, but not from oxaloacetate decarboxylase. 4. The intracellular localization of the NAD-linked "malic" enzyme was predominantly mitochondrial; latency studies suggested a localization in the mitochondrial matrix space. 5. Studies on the partially purified enzyme demonstrated that it had a pH optimum between 7.6 and 7.9. It required Mg2+ or Mn2+ for activity; Ca2+ was not effective. The maximum rate was the same with either cation, but the concentration of Mn2+ required was 100 times less than that of Mg2+. Acitivity with NADP was only 1-3% of that with NAD, unless very high (greater than 10mM) concentrations of Mn2+ were present. 6. It is suggested that the NAD-linked "malic" enzyme functions in the proline-oxidation pathway predominant in tse-tse fly flight muscle. | Nicotinamide-adenine dinucleotide-linked "malic" enzyme in flight muscle of the tse-tse fly (Glossina) and other insects. 1. A high activity of NAD-linked "malic" enzyme was found in homogenates of flight muscle of different species of tse-tse fly (Glossina). The activity was the same as, or higher than, that of malate dehydrogenase and more than 20-fold that of NADP-linked "malic" enzyme. A similar enzyme was found in the flight muscle of all other insects investigated, but at much lower activities. 2. ACa2+-stimulated oxaloacetate decarboxylase activity was present in all insect flight-muscle preparations investigated, in constant proportion to the NAD-linked "malic" enzyme. 3. A partial purification of the NAD-linked "malic" enzyme from Glossina was effected by DEAE-cellulose chromatography, which separated the enzyme from malate dehydrogenase and NADP-linked "malic" enzyme, but not from oxaloacetate decarboxylase. 4. The intracellular localization of the NAD-linked "malic" enzyme was predominantly mitochondrial; latency studies suggested a localization in the mitochondrial matrix space. 5. Studies on the partially purified enzyme demonstrated that it had a pH optimum between 7.6 and 7.9. It required Mg2+ or Mn2+ for activity; Ca2+ was not effective. The maximum rate was the same with either cation, but the concentration of Mn2+ required was 100 times less than that of Mg2+. Acitivity with NADP was only 1-3% of that with NAD, unless very high (greater than 10mM) concentrations of Mn2+ were present. 6. It is suggested that the NAD-linked "malic" enzyme functions in the proline-oxidation pathway predominant in tse-tse fly flight muscle. | [
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|
PMID:12752 | The electrophoretic properties and aggregation of mouse lymphoma cells, chinese-hamster fibroblasts and a somatic-cell hybrid. | 1. The electrophoretic mobilities of a mouse lymphoma cell, a Chinese-hamster fibroblast and a somatic-cell hybrid (also fibroblastic), produced by fusion of the hamster cell and a mouse lymphoma cell, were measured at 25 degrees C over a range of pH, concentration of Ca2+ ions and concentration of La3+ ions. 2. All the cells have pI at pH3.5. 3. Ca2+ ions decrease the mobilities and zeta potentials of the cells to zero in the range 1-100mM. 4. La3+ ions lower the mobilities and zeta potentials in the range 10 muM-1 mM, and the cells become positively charged above 1 mM. 5. The data are consistent with specific adsorption of La3+ ions on approx. 2 X 10(14) sites/m2 of cell surface with a free energy of approx. -37kJ/mol. 6. The effects of Ca2+, La3+ and ionic strength on the extent of aggregation of the cells and of neuraminidase-treated cells were studied. 7. Ca2+ ions do not markedly increase aggregation, whereas La3+ ions gave rise to extensive aggregation in the range 10 muM-1 mM, corresponding to the region of La3+ adsorption. 8. Both fibroblastic cell lines are aggregated at high ionic strength. 9. The fibroblastic cells have larger amounts of trypsin-sensitive carbohydrate than does the lymphoma cell; the possible role of this material in cellular aggregation is discussed. | The electrophoretic properties and aggregation of mouse lymphoma cells, chinese-hamster fibroblasts and a somatic-cell hybrid. 1. The electrophoretic mobilities of a mouse lymphoma cell, a Chinese-hamster fibroblast and a somatic-cell hybrid (also fibroblastic), produced by fusion of the hamster cell and a mouse lymphoma cell, were measured at 25 degrees C over a range of pH, concentration of Ca2+ ions and concentration of La3+ ions. 2. All the cells have pI at pH3.5. 3. Ca2+ ions decrease the mobilities and zeta potentials of the cells to zero in the range 1-100mM. 4. La3+ ions lower the mobilities and zeta potentials in the range 10 muM-1 mM, and the cells become positively charged above 1 mM. 5. The data are consistent with specific adsorption of La3+ ions on approx. 2 X 10(14) sites/m2 of cell surface with a free energy of approx. -37kJ/mol. 6. The effects of Ca2+, La3+ and ionic strength on the extent of aggregation of the cells and of neuraminidase-treated cells were studied. 7. Ca2+ ions do not markedly increase aggregation, whereas La3+ ions gave rise to extensive aggregation in the range 10 muM-1 mM, corresponding to the region of La3+ adsorption. 8. Both fibroblastic cell lines are aggregated at high ionic strength. 9. The fibroblastic cells have larger amounts of trypsin-sensitive carbohydrate than does the lymphoma cell; the possible role of this material in cellular aggregation is discussed. | [
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PMID:12753 | Mitochondrial adenosine triphosphatase of the fission yeast, Schizosaccharomyces pombe 972h-. Changes in activity and inhibitor-sensitivity in response to catabolite repression. | 1. The specific activity of mitochondrial ATPase (adenosine triphosphatase) in extracts of Schizosaccharomyces pombe decreased 2.5-fold as the glucose concentration in the growth medium decreased from 50mM to 15mM. 2. During the late exponential phase of growth, ATPase activity doubled. 3. Sensitivity to oligomycin and Dio-9 as measured by values for I50(mug of inhibitor/mg of protein giving 50% inhibition) at pH 6.8 increased sixfold and ninefold respectively during the initial decrease in ATPase activity, and this degree of sensitivity was maintained for the remainder of the growth cycle. 4. Increased sensitivity to NN'-dicyclohexylcarbodi-imide, triethyltin and venturicidin was also observed during the early stage of glucose de-repression. 5. Smaller increases in sensitivity to efrapeptin, aurovertin, 7-chloro-4-nitrobenzo-2-oxa-1,3-diaz-le, quercetin and spegazzinine also occurred. 6. The ATPase of glycerol-grown cells was less sensitive to inhibitors than that of glucose-repressed cells; change in values for I50 were not so marked during the growth cycle of cells growing with glycerol. 7. When submitochondrial particles from glycerol-grown cells were tested by passage through Sephadex G-50, a fourfold increase in activity was accompanied by increased inhibitor resistance. 8. Gel filtration of submitochondrial particles from glucose-de-repressed cells gave similar results, whereas loss of ATPase occurred in submitochondrial particles from glucose-repressed cells. 9. It is proposed that alterations in sensitivity to inhibitors at different stages of glucose derepression may be partly controlled by a naturally occuring inhibitor of ATPase. 10. The inhibitors tested may be classififed into two groups on the basis of alterations of sensitivity of the ATPase during physiological modification: (a) oligomycin, Dio-9, NN'-dicyclohexylcarbodi-imide, venturicidin and triethyltin, and (b) efrapeptin, aurovertin, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, quercetin and spegazzinine. | Mitochondrial adenosine triphosphatase of the fission yeast, Schizosaccharomyces pombe 972h-. Changes in activity and inhibitor-sensitivity in response to catabolite repression. 1. The specific activity of mitochondrial ATPase (adenosine triphosphatase) in extracts of Schizosaccharomyces pombe decreased 2.5-fold as the glucose concentration in the growth medium decreased from 50mM to 15mM. 2. During the late exponential phase of growth, ATPase activity doubled. 3. Sensitivity to oligomycin and Dio-9 as measured by values for I50(mug of inhibitor/mg of protein giving 50% inhibition) at pH 6.8 increased sixfold and ninefold respectively during the initial decrease in ATPase activity, and this degree of sensitivity was maintained for the remainder of the growth cycle. 4. Increased sensitivity to NN'-dicyclohexylcarbodi-imide, triethyltin and venturicidin was also observed during the early stage of glucose de-repression. 5. Smaller increases in sensitivity to efrapeptin, aurovertin, 7-chloro-4-nitrobenzo-2-oxa-1,3-diaz-le, quercetin and spegazzinine also occurred. 6. The ATPase of glycerol-grown cells was less sensitive to inhibitors than that of glucose-repressed cells; change in values for I50 were not so marked during the growth cycle of cells growing with glycerol. 7. When submitochondrial particles from glycerol-grown cells were tested by passage through Sephadex G-50, a fourfold increase in activity was accompanied by increased inhibitor resistance. 8. Gel filtration of submitochondrial particles from glucose-de-repressed cells gave similar results, whereas loss of ATPase occurred in submitochondrial particles from glucose-repressed cells. 9. It is proposed that alterations in sensitivity to inhibitors at different stages of glucose derepression may be partly controlled by a naturally occuring inhibitor of ATPase. 10. The inhibitors tested may be classififed into two groups on the basis of alterations of sensitivity of the ATPase during physiological modification: (a) oligomycin, Dio-9, NN'-dicyclohexylcarbodi-imide, venturicidin and triethyltin, and (b) efrapeptin, aurovertin, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, quercetin and spegazzinine. | [
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PMID:12754 | Oxygen toxicity in the perfused rat liver and lung under hyperbaric conditions. | 1. In the lung and liver of tocopherol-deficient rats, the activities of glutathione peroxidase and glucose 6-phosphate dehydrogenase were increased substantially, suggesting an important role for both enzymes in protecting the organ against the deleterious effects of lipid peroxides. 2. Facilitation of the glutathione peroxidase reaction by infusing t-butyl hydroperoxide caused the oxidation of nicotinamide nucleotides and glutathione, resulting in a concomitant increase in the rate of release of oxidized glutathione into the perfusate. Thus the rate of production of lipid peroxide and H2O2 in the perfused organ could be compared by simultaneous measurement of the rate of glutathione release and the turnover number of the catalase reaction. 3. On hyperbaric oxygenation at 4 X 10(5)Pa, H2O2 production, estimated from the turnover of the catalase reaction, was increased slightly in the liver, and glutathione release was increased slightly, in both lung and liver. 4. Tocopherol deficiency caused a marked increase in lipid-peroxide formation as indicated by a corresponding increase in glutathione release under hyperbaric oxygenation, with a further enhancement when the tocopherol-deficient rats were also starved. 5. The study demonstrates that the primary response to hyperbaric oxygenation is an elevation of the rate of lipid peroxidation rather than of the rate of formation of H2O2 or superoxide. | Oxygen toxicity in the perfused rat liver and lung under hyperbaric conditions. 1. In the lung and liver of tocopherol-deficient rats, the activities of glutathione peroxidase and glucose 6-phosphate dehydrogenase were increased substantially, suggesting an important role for both enzymes in protecting the organ against the deleterious effects of lipid peroxides. 2. Facilitation of the glutathione peroxidase reaction by infusing t-butyl hydroperoxide caused the oxidation of nicotinamide nucleotides and glutathione, resulting in a concomitant increase in the rate of release of oxidized glutathione into the perfusate. Thus the rate of production of lipid peroxide and H2O2 in the perfused organ could be compared by simultaneous measurement of the rate of glutathione release and the turnover number of the catalase reaction. 3. On hyperbaric oxygenation at 4 X 10(5)Pa, H2O2 production, estimated from the turnover of the catalase reaction, was increased slightly in the liver, and glutathione release was increased slightly, in both lung and liver. 4. Tocopherol deficiency caused a marked increase in lipid-peroxide formation as indicated by a corresponding increase in glutathione release under hyperbaric oxygenation, with a further enhancement when the tocopherol-deficient rats were also starved. 5. The study demonstrates that the primary response to hyperbaric oxygenation is an elevation of the rate of lipid peroxidation rather than of the rate of formation of H2O2 or superoxide. | [
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|
PMID:12755 | Acute effects in vivo of anti-insulin serum on rates of fatty acid synthesis and activities of acetyl-coenzyme A carboxylase and pyruvate dehydrogenase in liver and epididymal adipose tissue of fed rats. | Plasma insulin concentrations in fed rats were altered acutely by administration of glucose or anti-insulin serum. Rates of fatty acid synthesis in adipose tissue and liver were estimated from the incorporation of 3H from 3H2O. In the adipose tissue dehydrogenase and acetyl-CoA carboxylase were evident. In liver, although changes in rates of fatty acid synthesis were found, the initial activity of pyruvate dehydrogenase did not alter, but small parallel changes in acetyl-CoA carboxylase activity were observed. | Acute effects in vivo of anti-insulin serum on rates of fatty acid synthesis and activities of acetyl-coenzyme A carboxylase and pyruvate dehydrogenase in liver and epididymal adipose tissue of fed rats. Plasma insulin concentrations in fed rats were altered acutely by administration of glucose or anti-insulin serum. Rates of fatty acid synthesis in adipose tissue and liver were estimated from the incorporation of 3H from 3H2O. In the adipose tissue dehydrogenase and acetyl-CoA carboxylase were evident. In liver, although changes in rates of fatty acid synthesis were found, the initial activity of pyruvate dehydrogenase did not alter, but small parallel changes in acetyl-CoA carboxylase activity were observed. | [
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|
PMID:12764 | [Investigations on the Stability of Proscillaridine, Proscillaridine-3'-methylether and Proscillaridine-4'-methylether in Artificial Gastric and Intestinal Fluids (author's transl)]. | The stability of bufadienolides in artificial gastric and intestinal fluids was investigated at different pH-values as a function of incubation time using proscillaridine, proscillaridine-3'-methylether and proscillaridine-4'-methylether. These glycosides were completely stable on pH 3.0--8.5 during the investigated time interval of 1 h. At lower pH-values cleavage of the glycosidic bond occurred. At pH 1.0 73% of proscillaridine, 33% of proscillaridine-3'-methylether and 41% of proscillaridine-4'-methylether were decomposed. At pH 2.0 only about 10% decomposition of these compounds could be detected. These experiments show that the stability of proscillaridine in gastric juice is comparable with the stability of digitalis glycosides and digoxin derivatives. The stability of methylated proscillaridine derivatives in artificial digestion fluids, however, proved to be superior to any orally administered cardiac glycoside. | [Investigations on the Stability of Proscillaridine, Proscillaridine-3'-methylether and Proscillaridine-4'-methylether in Artificial Gastric and Intestinal Fluids (author's transl)]. The stability of bufadienolides in artificial gastric and intestinal fluids was investigated at different pH-values as a function of incubation time using proscillaridine, proscillaridine-3'-methylether and proscillaridine-4'-methylether. These glycosides were completely stable on pH 3.0--8.5 during the investigated time interval of 1 h. At lower pH-values cleavage of the glycosidic bond occurred. At pH 1.0 73% of proscillaridine, 33% of proscillaridine-3'-methylether and 41% of proscillaridine-4'-methylether were decomposed. At pH 2.0 only about 10% decomposition of these compounds could be detected. These experiments show that the stability of proscillaridine in gastric juice is comparable with the stability of digitalis glycosides and digoxin derivatives. The stability of methylated proscillaridine derivatives in artificial digestion fluids, however, proved to be superior to any orally administered cardiac glycoside. | [
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|
PMID:12765 | Piroxicam, a novel anti-inflammatory agent. | Piroxicam (CP-16 171) is a potent acidic anti-inflammatory agent structurally distinct from the current agents such as indometacin, phenylbutazone or naproxen. Pharmacokinetic studies indicate a longer plasma half-ife for piroxicam than for these agents. Potency in the range of indometacin is observed when piroxicam is tested in the carrageenan rat paw edema model. This activity is not dependent on an intact adrenocorticoid system. The high potency, long half-life and absence of cardiovascular or cental nervous system effects have encouraged clinical trial of piroxicam. | Piroxicam, a novel anti-inflammatory agent. Piroxicam (CP-16 171) is a potent acidic anti-inflammatory agent structurally distinct from the current agents such as indometacin, phenylbutazone or naproxen. Pharmacokinetic studies indicate a longer plasma half-ife for piroxicam than for these agents. Potency in the range of indometacin is observed when piroxicam is tested in the carrageenan rat paw edema model. This activity is not dependent on an intact adrenocorticoid system. The high potency, long half-life and absence of cardiovascular or cental nervous system effects have encouraged clinical trial of piroxicam. | [
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|
PMID:12766 | Cardiorespiratory activitirs of 3-formylamino-4-hydroxy-alpha-(n-1-methyl-2-p-methoxyphenethylaminomethyl)-benzylalcohol-hemifumarate(BD 40A) and some other beta-adrenoceptor stimulants in conscious guinea pigs. | The beta-stimulant activity of 3-formylamino-4-hydroxy-alpha-(N-1-methoxyphenethylaminomethyl)-benzylalcohol-hemifumarate (BD 40A) was compared with those of isoproterenol, orciprenaline, trimetoquinol and salbutamol in conscious guinea pigs. Bronchodilator effects of BD 40A were most potent among five agonists by s.c., oral and aerosol administration, and were lasting by oral and aerosol administration. BD 40A was similar to isoproterenol, more potent than trimetoquinol, orciprenaline and salbutamol in increasing heart rate by s.c. route. The cardiostimulating effect of BD 40A was more potent than that of isoproterenol, trimetoquinol and salbutamol orally. However, the order of bronchoselectivity (ratio between ED30 beats/min vs. ED50) in conscious guinea pigs was salbutamol greater than BD 40A = trimetoquinol greater than orciprenaline greater than isoproterenol by s.c. administration, and by oral administration the order was BD 40A = salbutamol greater than trimetoquinol = isoproterenol. Orciprenaline showed no beta-stimulating effect in guinea pigs orally. In guinea pigs, BD 40A, like salbutamol, seems to be a beta2-adrenoceptor stimulant. | Cardiorespiratory activitirs of 3-formylamino-4-hydroxy-alpha-(n-1-methyl-2-p-methoxyphenethylaminomethyl)-benzylalcohol-hemifumarate(BD 40A) and some other beta-adrenoceptor stimulants in conscious guinea pigs. The beta-stimulant activity of 3-formylamino-4-hydroxy-alpha-(N-1-methoxyphenethylaminomethyl)-benzylalcohol-hemifumarate (BD 40A) was compared with those of isoproterenol, orciprenaline, trimetoquinol and salbutamol in conscious guinea pigs. Bronchodilator effects of BD 40A were most potent among five agonists by s.c., oral and aerosol administration, and were lasting by oral and aerosol administration. BD 40A was similar to isoproterenol, more potent than trimetoquinol, orciprenaline and salbutamol in increasing heart rate by s.c. route. The cardiostimulating effect of BD 40A was more potent than that of isoproterenol, trimetoquinol and salbutamol orally. However, the order of bronchoselectivity (ratio between ED30 beats/min vs. ED50) in conscious guinea pigs was salbutamol greater than BD 40A = trimetoquinol greater than orciprenaline greater than isoproterenol by s.c. administration, and by oral administration the order was BD 40A = salbutamol greater than trimetoquinol = isoproterenol. Orciprenaline showed no beta-stimulating effect in guinea pigs orally. In guinea pigs, BD 40A, like salbutamol, seems to be a beta2-adrenoceptor stimulant. | [
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|
PMID:12767 | [The influence of pentagastrin on the ratios of Na+,K+H+/Amino acids in gastric juice. Short communication (author's transl)]. | Pentagastrin has a distinct effect on the ratios of Na+,K+,H+/amino acid in the gastric juice in the different states of acidity. Contrary to the ratios of normacidity the values of all quotients in patients with hyper-, hypo- and anacidity are significantly reduced. | [The influence of pentagastrin on the ratios of Na+,K+H+/Amino acids in gastric juice. Short communication (author's transl)]. Pentagastrin has a distinct effect on the ratios of Na+,K+,H+/amino acid in the gastric juice in the different states of acidity. Contrary to the ratios of normacidity the values of all quotients in patients with hyper-, hypo- and anacidity are significantly reduced. | [
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|
PMID:12768 | [Profile of pharmacological actions of NAB 365 (clenbuterol), a novel broncholytic agent with selective activity on adrenergic beta2-receptors (author's transl)]. | Effects of 4-amino-alpha-[(tert.-butylamino)methyl]-3,5-dichlorobenzyl alcohol hydrochloride (clenbuterol, NAB 365) on the adrenergic beta-receptors were investigated and compared with those of isoproterenol and salbutamol. The beta2-mimetic activity of clenbuterol on the smooth muscle of bronchi, uterus and vessels after i.v. injection corresponds to that of salbutamol in all laboratory animals. When given subcutaneously or as an aerosol clenbuterol is even somewhat more effective than isoproterenol. Clenbuterol differs from the known beta-mimetic drugs in its much longer duration of action. Therefore the integral of activity of single doses of clenbuterol, which are equally effective in the period of their maximal action, is remarkably greater than that of the other beta-mimetic substances. Clenbuterol differs from known beta-mimetic drugs used as bronchodilators in its efficacy after oral administration and in its mode of action on the heart. In the isolated auricle of the rabbit it has proved to be a weak partial agonist. In conscious rabbits, anesthetised guinea-pigs, dogs and cats the maximum of tachycardia obtainable by clenbuterol is lower than that of salbutamol. The higher degree of tachycardia in conscious dogs provoked by clenbuterol is a result of a reflex reaction to the vasodilation analogous to that of salbutamol. In higher doses clenbuterol shows beta1-blocking properties. Like other beta-blocking agents it owns qualities of a local-anesthetic and prolongs refractory period of the heart of guinea-pigs. In contrast to other beta-mimetic substances, clenbuterol causes only slight mobilization of heart muscle glycogen by doses higher than those which have broncholytic effects. The lipolytic and lactacidemia inducing activity of clenbuterol in rabbits corresponds to that of isoproterenol. The blood sugar is only slightly increased by clenbuterol as well as by other beta-mimetic agents. Degree and duration of action of clenbuterol and the other sympathomimetic amines on skeletal muscle of the cat shows parallelism with that of the broncholytic effect. In the rat clenbuterol inhibits the gastric secretion more than does isoproterenol. In contrast to other broncholytic substances, a very small dosage of clenbuterol is sufficient to protect rats against the liberation of histamine and serotonin caused by the anaphylactic reaction. | [Profile of pharmacological actions of NAB 365 (clenbuterol), a novel broncholytic agent with selective activity on adrenergic beta2-receptors (author's transl)]. Effects of 4-amino-alpha-[(tert.-butylamino)methyl]-3,5-dichlorobenzyl alcohol hydrochloride (clenbuterol, NAB 365) on the adrenergic beta-receptors were investigated and compared with those of isoproterenol and salbutamol. The beta2-mimetic activity of clenbuterol on the smooth muscle of bronchi, uterus and vessels after i.v. injection corresponds to that of salbutamol in all laboratory animals. When given subcutaneously or as an aerosol clenbuterol is even somewhat more effective than isoproterenol. Clenbuterol differs from the known beta-mimetic drugs in its much longer duration of action. Therefore the integral of activity of single doses of clenbuterol, which are equally effective in the period of their maximal action, is remarkably greater than that of the other beta-mimetic substances. Clenbuterol differs from known beta-mimetic drugs used as bronchodilators in its efficacy after oral administration and in its mode of action on the heart. In the isolated auricle of the rabbit it has proved to be a weak partial agonist. In conscious rabbits, anesthetised guinea-pigs, dogs and cats the maximum of tachycardia obtainable by clenbuterol is lower than that of salbutamol. The higher degree of tachycardia in conscious dogs provoked by clenbuterol is a result of a reflex reaction to the vasodilation analogous to that of salbutamol. In higher doses clenbuterol shows beta1-blocking properties. Like other beta-blocking agents it owns qualities of a local-anesthetic and prolongs refractory period of the heart of guinea-pigs. In contrast to other beta-mimetic substances, clenbuterol causes only slight mobilization of heart muscle glycogen by doses higher than those which have broncholytic effects. The lipolytic and lactacidemia inducing activity of clenbuterol in rabbits corresponds to that of isoproterenol. The blood sugar is only slightly increased by clenbuterol as well as by other beta-mimetic agents. Degree and duration of action of clenbuterol and the other sympathomimetic amines on skeletal muscle of the cat shows parallelism with that of the broncholytic effect. In the rat clenbuterol inhibits the gastric secretion more than does isoproterenol. In contrast to other broncholytic substances, a very small dosage of clenbuterol is sufficient to protect rats against the liberation of histamine and serotonin caused by the anaphylactic reaction. | [
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|
PMID:12769 | Synthetic analgesics: N-(1-[2-arylethyl]-4-substituted 4-piperidinyl) N-arylalkanamides. | The synthesis of several 4-arylamino-4-piperdinecarboxylic acids is reported. These acids were starting materials for the preparation of alpha-amino esthers, ethers and ketones. Different synthetic approaches are described. Suitable substitution on both nitrogen atoms afforded extremely potent analgesics. Thus, methyl 4-[N-(1-oxopropyl)-N-phenylamino]-1-(2-phenylethyl)-4-piperidinecarboxylate (22),N-(4-(methoxymethyl)-2-[2-(2-thienyl)ethyl]-4-piperidinyl)-N-phenylpropranamide (67) and N-[4-acetyl-1-(2-phenylethyl)-4-piperidinyl]-N-phenylpropanamide (82) were found to be respectively 7682, 3987 and 4921 times as potent as morfine. Both cis- and trans-3-methyl homologs of 22 have been prepared. As expected, analgesic activity resides mainly in the cis-isomer. | Synthetic analgesics: N-(1-[2-arylethyl]-4-substituted 4-piperidinyl) N-arylalkanamides. The synthesis of several 4-arylamino-4-piperdinecarboxylic acids is reported. These acids were starting materials for the preparation of alpha-amino esthers, ethers and ketones. Different synthetic approaches are described. Suitable substitution on both nitrogen atoms afforded extremely potent analgesics. Thus, methyl 4-[N-(1-oxopropyl)-N-phenylamino]-1-(2-phenylethyl)-4-piperidinecarboxylate (22),N-(4-(methoxymethyl)-2-[2-(2-thienyl)ethyl]-4-piperidinyl)-N-phenylpropranamide (67) and N-[4-acetyl-1-(2-phenylethyl)-4-piperidinyl]-N-phenylpropanamide (82) were found to be respectively 7682, 3987 and 4921 times as potent as morfine. Both cis- and trans-3-methyl homologs of 22 have been prepared. As expected, analgesic activity resides mainly in the cis-isomer. | [
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PMID:12770 | In vitro effects of bencyclan on coagulation, fibrinolysis and platelet function. | The in vitro effects of N-3-(1-benzyl-cycloheptyloxy)-propyl-N,N-dimethylammonium-hydrogenfumarate (bencyclan) on clotting, fibrinolytic and platelet function test were investigated by adding the drug to normal human plasma. An anticoagulant activity, mainly of an antithromboplastin nature (directed against later stages of intrinsic thromboplastin formation and against tissue thromboplastin), was observed, while thrombin phase was unaffected. No effect was found in the fibrinolytic system tested (euglobulin lysis, UK-activated fibrinolysis, "hanging clot" method). The drug, although capable of aggregating platelets by itself at very high concentrations, showed a striking inhibitory effect, over a wide range of concentrations, both on platelet aggregation induced by ADP, epinephrine or collagen and on platelet adhesiveness to glass or collagen. Clot retraction was also clearly inhibited. PF3 availability was influenced with a peculiar two-phase behaviour dose-dependently. High concentrations showed a promoting action, while the lower were obviously inhibitory. It is suggested that the effects on platelet function may be due to an influence of the drug on cell membrane. | In vitro effects of bencyclan on coagulation, fibrinolysis and platelet function. The in vitro effects of N-3-(1-benzyl-cycloheptyloxy)-propyl-N,N-dimethylammonium-hydrogenfumarate (bencyclan) on clotting, fibrinolytic and platelet function test were investigated by adding the drug to normal human plasma. An anticoagulant activity, mainly of an antithromboplastin nature (directed against later stages of intrinsic thromboplastin formation and against tissue thromboplastin), was observed, while thrombin phase was unaffected. No effect was found in the fibrinolytic system tested (euglobulin lysis, UK-activated fibrinolysis, "hanging clot" method). The drug, although capable of aggregating platelets by itself at very high concentrations, showed a striking inhibitory effect, over a wide range of concentrations, both on platelet aggregation induced by ADP, epinephrine or collagen and on platelet adhesiveness to glass or collagen. Clot retraction was also clearly inhibited. PF3 availability was influenced with a peculiar two-phase behaviour dose-dependently. High concentrations showed a promoting action, while the lower were obviously inhibitory. It is suggested that the effects on platelet function may be due to an influence of the drug on cell membrane. | [
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PMID:12771 | N-4-Substituted 1-(2-arylethyl)-4-piperidinyl-N-phenylpropanamides, a novel series of extremely potent analgesics with unusually high safety margin. | The intravenous analgesic activity and toxicity of a novel series of N-[4-substituted 1-(2-arylethyl)-4-piperidinyl]-N-phenylpropanamides was studied in rats. Onset, potency and duration of analgesic action were assessed in the tail withdrawal test and compared with the activity of fentanyl, (+)-cis-3-methylfentanyl (R 26 800), morphine, and pethidine. All compounds studied were found to be extremely potent analgesics characterized by an unusually high safety margin. Methyl 4-[N-(1-oxopropyl)-N-phenyl-amino]-1-(2-phenylethyl)-4-piperidinecarboxylate (R 31 833; lowest ED50 = 0.00032 mg/kg) is the most potent compound (10 031 times morphine). cis-Methyl 3-methyl-4-[N-(1-oxopropyl)-N-phenylamino]-1-(2-phenylethyl)-4-piperidine carboxylate (R 32 792) is the longest acting compound (more than 8 h at 4 times the lowest ED50) and N-[4-(1-oxopropyl)-1-[2-(2-thienyl)ethyl]-4-piperidinyl]-N-phenylpropanamide (R 33 352) is the shortest acting compound (0.74 h at 4 times the lowest ED50) of the 4-substituted fentanyl derivatives. N-[4-(Methoxymethyl)-1-[2-(2-thienyl)ethyl]-4-piperidinyl]-N-phenylpropanamide (R 30 730) was selected for further investigation. R 30 730 has a rapid onset of action and is 4521 times more potent than morphine at the time of peak effect; it has a relatively short duration of action comparable to that of fentanyl and its safety margin (LD50/lowest ED50 = 25 211) is unusually high. | N-4-Substituted 1-(2-arylethyl)-4-piperidinyl-N-phenylpropanamides, a novel series of extremely potent analgesics with unusually high safety margin. The intravenous analgesic activity and toxicity of a novel series of N-[4-substituted 1-(2-arylethyl)-4-piperidinyl]-N-phenylpropanamides was studied in rats. Onset, potency and duration of analgesic action were assessed in the tail withdrawal test and compared with the activity of fentanyl, (+)-cis-3-methylfentanyl (R 26 800), morphine, and pethidine. All compounds studied were found to be extremely potent analgesics characterized by an unusually high safety margin. Methyl 4-[N-(1-oxopropyl)-N-phenyl-amino]-1-(2-phenylethyl)-4-piperidinecarboxylate (R 31 833; lowest ED50 = 0.00032 mg/kg) is the most potent compound (10 031 times morphine). cis-Methyl 3-methyl-4-[N-(1-oxopropyl)-N-phenylamino]-1-(2-phenylethyl)-4-piperidine carboxylate (R 32 792) is the longest acting compound (more than 8 h at 4 times the lowest ED50) and N-[4-(1-oxopropyl)-1-[2-(2-thienyl)ethyl]-4-piperidinyl]-N-phenylpropanamide (R 33 352) is the shortest acting compound (0.74 h at 4 times the lowest ED50) of the 4-substituted fentanyl derivatives. N-[4-(Methoxymethyl)-1-[2-(2-thienyl)ethyl]-4-piperidinyl]-N-phenylpropanamide (R 30 730) was selected for further investigation. R 30 730 has a rapid onset of action and is 4521 times more potent than morphine at the time of peak effect; it has a relatively short duration of action comparable to that of fentanyl and its safety margin (LD50/lowest ED50 = 25 211) is unusually high. | [
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PMID:12772 | Sufentanil, a very potent and extremely safe intravenous morphine-like compound in mice, rats and dogs. | Sufentanil (R 30 730), N-[4-methoxymethyl)-1-[2-(2-thienyl)ethyl]-4-piperidinyl]-N-phenylpropanamide, is a chemically novel, highly potent and extremely safe intravenous morphine-like agent in laboratory animals. In mice R 30 730 i.v. is 2304 times more potent than morphine (hot plate ED50's: 0.0028 and 6.45 mg/kg, respectively). The i.v. safety margin of R 30 730 in mice is 1 : 6 679 (LD50 = 18.7 mg/kg). Under the same experimental conditions the safety margin of pethidine is 1 : 7.97, of morphine 1 : 34.9 and of fentanyl 1 : 454. In rats R 30 730 i.v. is 4521 times more potent than morphine (tail withdrawal test ED50's: 0.00071 and 3.21 mg/kg, respectively). The i.v. safety margin of R 30 730 in rats is 1 : 25 211 (LD50 : 17.9 mg/kg). Under the latter experimental conditions the safety margin of pethidine is 1 : 4.80, of morphine 1 : 69.5 and of fentanyl 1 : 277. In dogs R 30 730 i.v. is 2429 times more potent than morphine (apomorphine antagonism test ED50's: 0.00028 and 0.68 mg/kg, respectively). The i.v. safety margin in dogs is approximately 1 : 50 000, the LD50 being +/- 14.0 mg/kg. All morphine-like effects of R 30 730 are immediately antagonized by nalorphine. These pharmacological findings are relevant in connection to the increasing interest for use of morphinomimetics in anesthesia. | Sufentanil, a very potent and extremely safe intravenous morphine-like compound in mice, rats and dogs. Sufentanil (R 30 730), N-[4-methoxymethyl)-1-[2-(2-thienyl)ethyl]-4-piperidinyl]-N-phenylpropanamide, is a chemically novel, highly potent and extremely safe intravenous morphine-like agent in laboratory animals. In mice R 30 730 i.v. is 2304 times more potent than morphine (hot plate ED50's: 0.0028 and 6.45 mg/kg, respectively). The i.v. safety margin of R 30 730 in mice is 1 : 6 679 (LD50 = 18.7 mg/kg). Under the same experimental conditions the safety margin of pethidine is 1 : 7.97, of morphine 1 : 34.9 and of fentanyl 1 : 454. In rats R 30 730 i.v. is 4521 times more potent than morphine (tail withdrawal test ED50's: 0.00071 and 3.21 mg/kg, respectively). The i.v. safety margin of R 30 730 in rats is 1 : 25 211 (LD50 : 17.9 mg/kg). Under the latter experimental conditions the safety margin of pethidine is 1 : 4.80, of morphine 1 : 69.5 and of fentanyl 1 : 277. In dogs R 30 730 i.v. is 2429 times more potent than morphine (apomorphine antagonism test ED50's: 0.00028 and 0.68 mg/kg, respectively). The i.v. safety margin in dogs is approximately 1 : 50 000, the LD50 being +/- 14.0 mg/kg. All morphine-like effects of R 30 730 are immediately antagonized by nalorphine. These pharmacological findings are relevant in connection to the increasing interest for use of morphinomimetics in anesthesia. | [
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|
PMID:12773 | [Blood gas analytical study on cerebral circulation under the influence of dihydroergotoxin (author's transl)]. | The demand for sufficient blood supply and oxygenation of cerebral tissue after brain surgery or severe head injuries requires the clinical investigation of drugs which are supposed to improve cerebral blood flow and metabolism. We have therefore used the hydrogenated derivatives of the ergotoxin components of the secale alcaloids in the post-operative and posttraumatic period of neurosurgical patients, respectively, and studied their effect on cerebral metabolism by successive analysis of blood gases in the arterial and venous blood. A significant increase of cerebral venous CO2-concentration following the administration of dihydroergotoxin in these patients in all probability is attributable to an improved O2-utilisation in the cerebral tissue. | [Blood gas analytical study on cerebral circulation under the influence of dihydroergotoxin (author's transl)]. The demand for sufficient blood supply and oxygenation of cerebral tissue after brain surgery or severe head injuries requires the clinical investigation of drugs which are supposed to improve cerebral blood flow and metabolism. We have therefore used the hydrogenated derivatives of the ergotoxin components of the secale alcaloids in the post-operative and posttraumatic period of neurosurgical patients, respectively, and studied their effect on cerebral metabolism by successive analysis of blood gases in the arterial and venous blood. A significant increase of cerebral venous CO2-concentration following the administration of dihydroergotoxin in these patients in all probability is attributable to an improved O2-utilisation in the cerebral tissue. | [
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|
PMID:12774 | Failure of benzoctamine to influence the activity of rat striatum tyrosine-hydroxylase. | The influence of benzoctamine (Tacitin) on rat striatum tyrosine-hydroxylase was analized. Injection of 100 mg benzoctamine/kg body weight caused no alteration in the tyrosine-hydroxylase activity whilst a decrease of about 60% in the activity was recorded after treatment with a-methyl-p-tyrosine a known inhibitor of tyrosine-hydroxylase. The present results differ from those of Maitre et al. which indicated that benzoctamine inhibited tyrosine-hydroxylase activity. | Failure of benzoctamine to influence the activity of rat striatum tyrosine-hydroxylase. The influence of benzoctamine (Tacitin) on rat striatum tyrosine-hydroxylase was analized. Injection of 100 mg benzoctamine/kg body weight caused no alteration in the tyrosine-hydroxylase activity whilst a decrease of about 60% in the activity was recorded after treatment with a-methyl-p-tyrosine a known inhibitor of tyrosine-hydroxylase. The present results differ from those of Maitre et al. which indicated that benzoctamine inhibited tyrosine-hydroxylase activity. | [
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|
PMID:12778 | Pharmacological basis for antihypertensive effects of intravenous labetalol. | Labetalol 1-5 mg/kg administered intravenously to normal subjects in the supine position produced an immediate mean fall in systolic (16%) and diastolic (25%) blood pressure with a concomitant increase in heart rate (12%). After graded exercise, intravenous labetalol inhibited increases in heart rate and blood pressure. Isoprenaline log dose response curves of increase in heart rate and reduction in diastolic pressure after intravenous labetalol shifted to the right in a parallel manner compared with pre-labetalol response curves suggestive of competitive antagonism at beta-adrenoceptor sites. Similarly, phenylephrine dose response curves of increase in systolic pressure before and after intravenous labetalol were suggestive of competitive antagonism at alpha-adrenoceptor sites. The ratio of relative potency alpha: beta adrenoceptor antagonism after intravenous labetalol was approximately 1:7, whereas in the same subjects after oral labetalol the ratio was approximately 1:3 as previously reported. Using the inhibition of isoprenaline tachycardia to estimate the potency of the beta-adrenoceptor antagonism of labetalol relative to that of propranolol the potency ratio was 1:6. However, using inhibition of Valsalva tachycardia as the index, the estimated ratio was approximately 1:3. Estimates of relative potency using inhibition of tilt tachycardia were complicated by the additional effects upon blood pressure after labetalol not seen after propranolol. Labetalol produced adrenoceptor blockade at both alpha and beta sites in man sufficient to explain its therapeutic antihypertensive effect. | Pharmacological basis for antihypertensive effects of intravenous labetalol. Labetalol 1-5 mg/kg administered intravenously to normal subjects in the supine position produced an immediate mean fall in systolic (16%) and diastolic (25%) blood pressure with a concomitant increase in heart rate (12%). After graded exercise, intravenous labetalol inhibited increases in heart rate and blood pressure. Isoprenaline log dose response curves of increase in heart rate and reduction in diastolic pressure after intravenous labetalol shifted to the right in a parallel manner compared with pre-labetalol response curves suggestive of competitive antagonism at beta-adrenoceptor sites. Similarly, phenylephrine dose response curves of increase in systolic pressure before and after intravenous labetalol were suggestive of competitive antagonism at alpha-adrenoceptor sites. The ratio of relative potency alpha: beta adrenoceptor antagonism after intravenous labetalol was approximately 1:7, whereas in the same subjects after oral labetalol the ratio was approximately 1:3 as previously reported. Using the inhibition of isoprenaline tachycardia to estimate the potency of the beta-adrenoceptor antagonism of labetalol relative to that of propranolol the potency ratio was 1:6. However, using inhibition of Valsalva tachycardia as the index, the estimated ratio was approximately 1:3. Estimates of relative potency using inhibition of tilt tachycardia were complicated by the additional effects upon blood pressure after labetalol not seen after propranolol. Labetalol produced adrenoceptor blockade at both alpha and beta sites in man sufficient to explain its therapeutic antihypertensive effect. | [
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|
PMID:12775 | Diffusion coefficients for protein molecules in blood serum. | A new technique is described for the measurement of the self-diffusion coefficients of protein macromolecules in solution. The method makes use of the phenomenon of Taylor dispersion of a solute introduced into a solvent flowing in the laminar regime through a tube of circular section. Results are reported for the self-diffusion coefficient of cholesterol associated with lipoprotein molecules in dogs' serum at pH 7.4 in the temperature range 18-37 degrees C. The diffusivity of bovine serum albumin in serum has also been studied as a function of temperature at pH 7.4 and 4.7. In the more basic solution, measurements of the diffusivity as a function of protein concentration substantially agree with earlier work. For all the systems studied the diffusivity varies rapidly with temperature. The pH of the solution, in the case of bovine serum albumin, also has a significant effect on the diffusivity of the macromolecule. The latter observation is related to the amount of water bound to the protein molecule in solution. | Diffusion coefficients for protein molecules in blood serum. A new technique is described for the measurement of the self-diffusion coefficients of protein macromolecules in solution. The method makes use of the phenomenon of Taylor dispersion of a solute introduced into a solvent flowing in the laminar regime through a tube of circular section. Results are reported for the self-diffusion coefficient of cholesterol associated with lipoprotein molecules in dogs' serum at pH 7.4 in the temperature range 18-37 degrees C. The diffusivity of bovine serum albumin in serum has also been studied as a function of temperature at pH 7.4 and 4.7. In the more basic solution, measurements of the diffusivity as a function of protein concentration substantially agree with earlier work. For all the systems studied the diffusivity varies rapidly with temperature. The pH of the solution, in the case of bovine serum albumin, also has a significant effect on the diffusivity of the macromolecule. The latter observation is related to the amount of water bound to the protein molecule in solution. | [
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|
PMID:12776 | [Acid-base equilibrium in healthy newborns. Pattern of normality in Mexico City]. | During their spontaneous recovery after birth, the acid-base balance was studied in 32 healthy newborns. The observation period lasted for 4 hours. Determinations were carried out, both in umbilical vessels as in central arterial blood. The most outstanding phenomenon was an increase in acidosis at 30 minutes of life. The metabolic component predominating over the respiratory was a definitely evident fact. At the end of four hours, the acid-base balance reached figures considered normal for the adult. | [Acid-base equilibrium in healthy newborns. Pattern of normality in Mexico City]. During their spontaneous recovery after birth, the acid-base balance was studied in 32 healthy newborns. The observation period lasted for 4 hours. Determinations were carried out, both in umbilical vessels as in central arterial blood. The most outstanding phenomenon was an increase in acidosis at 30 minutes of life. The metabolic component predominating over the respiratory was a definitely evident fact. At the end of four hours, the acid-base balance reached figures considered normal for the adult. | [
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|
PMID:12780 | The effects of Bordetella pertussis vaccine on cerebral vascular permeability. | The effect of Bordetella pertussis vaccine on the cerebral vascular permeability in the mouse was studied by a radio-isotope method (131I-labelled HSA). Intravenous injection of 4 x 1010 heat-killed pertussis organisms caused a measurable increase in permeability in normal mice. Cryoinjury to the cerebral hemispheres resulted in a striking increase in vascular permeability at 24 h. This declined within 48 h and stabilized at a level fractionally higher than normal at 7 days ("healed lesion"). When pertussis organisms were injected into mice bearing ("healed lesion"). When pertussis organisms were injected into mice bearing "healed lesions" the increase in permeability was similar in magnitude to that in uninjured brain. The effect was increased by a second administration of pertussis 24 h after the first. The action of pertussis on a newly inflicted cryoinjury was protective. It is suggested that permeability changes in the cerebral vessels may be involved in the evolution of the encephalopathy attributed to the use of Bordetella pertussis vaccine in man. | The effects of Bordetella pertussis vaccine on cerebral vascular permeability. The effect of Bordetella pertussis vaccine on the cerebral vascular permeability in the mouse was studied by a radio-isotope method (131I-labelled HSA). Intravenous injection of 4 x 1010 heat-killed pertussis organisms caused a measurable increase in permeability in normal mice. Cryoinjury to the cerebral hemispheres resulted in a striking increase in vascular permeability at 24 h. This declined within 48 h and stabilized at a level fractionally higher than normal at 7 days ("healed lesion"). When pertussis organisms were injected into mice bearing ("healed lesion"). When pertussis organisms were injected into mice bearing "healed lesions" the increase in permeability was similar in magnitude to that in uninjured brain. The effect was increased by a second administration of pertussis 24 h after the first. The action of pertussis on a newly inflicted cryoinjury was protective. It is suggested that permeability changes in the cerebral vessels may be involved in the evolution of the encephalopathy attributed to the use of Bordetella pertussis vaccine in man. | [
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|
PMID:12781 | Inhibition of the liver and plasma protein acute-phase response in mice by D-galactosamine. | Local inflammation evoked in Swiss albino mice by subcutaneous injection of Celite resulted in a rise of liver tyrosine aminotransferase activity and plasma level of fibrinogen and seromucoid, while liver alanine aminotransferase activity and plasma level of fibrinogen and seromucoid, while liver alanine aminotransferase activity and the plasma level of albumin and total protein remained unaltered. By measuring the incorporation of [14C] leucine, stimulation of liver and plasms protein synthesis by Celite injection was demonstrated. Administration of D-galactosamine (2-5 mg/10 g body weight) inhibited the enhanced synthesis of liver proteins, and especially of trauma-induced synthesis of plasma fibrinogen and seromucoid. The inhibitory effect of galactosamine was most pronounced when the amino sugar was injected simultaneously with Celite and then protein synthesis was measured 6 h later. The results obtained support the idea that high doses of galactosamine inhibit transcription of trauma-inducible mRNA in the liver and thus block the acute-phase response. | Inhibition of the liver and plasma protein acute-phase response in mice by D-galactosamine. Local inflammation evoked in Swiss albino mice by subcutaneous injection of Celite resulted in a rise of liver tyrosine aminotransferase activity and plasma level of fibrinogen and seromucoid, while liver alanine aminotransferase activity and plasma level of fibrinogen and seromucoid, while liver alanine aminotransferase activity and the plasma level of albumin and total protein remained unaltered. By measuring the incorporation of [14C] leucine, stimulation of liver and plasms protein synthesis by Celite injection was demonstrated. Administration of D-galactosamine (2-5 mg/10 g body weight) inhibited the enhanced synthesis of liver proteins, and especially of trauma-induced synthesis of plasma fibrinogen and seromucoid. The inhibitory effect of galactosamine was most pronounced when the amino sugar was injected simultaneously with Celite and then protein synthesis was measured 6 h later. The results obtained support the idea that high doses of galactosamine inhibit transcription of trauma-inducible mRNA in the liver and thus block the acute-phase response. | [
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PMID:12782 | Atenolol versus propranolol. A comparison of ocular hypotensive effect of an oral dose. | In a controlled double-blind cross-over trial in 10 patients comprising six with open-angle glaucoma, three with closed-angle glaucoma, and one with ocular hypertension, a single oral dose of atenolol (50 mg) was significantly more effective than propranolol (40 mg) in reducing ocular tension. | Atenolol versus propranolol. A comparison of ocular hypotensive effect of an oral dose. In a controlled double-blind cross-over trial in 10 patients comprising six with open-angle glaucoma, three with closed-angle glaucoma, and one with ocular hypertension, a single oral dose of atenolol (50 mg) was significantly more effective than propranolol (40 mg) in reducing ocular tension. | [
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|
PMID:12783 | Milk-substitute diet composition and abomasal secretion in the calf. | 1. The effect of different protein sources in milk-substitute diets on abomasal acidity and proteolytic activity was studied in Friesian calves, aged 20-58 d (Expt 1). The diets contained 'mildly' preheated, spray-dried skim-milk powder (MHM), severely preheated, spray-dried skim-milk powder (SHM), fish-protein concentrate (FPC) or solvent-extracted soya-bean flour (SF) as the main protein source. 2. Gastric juice was collected from abomasal pouches before feeding and at 15 min intervals for 8 h after the morning feed. Samples of digesta were obtained from the abomasum at 1 h intervals during the same period. 3. Digesta pH was lower and titratable acidity higher 0-3 after giving the diet containing MHM than when any of the other three diets was given. 3. Acid secretion from the pouches for the different diets was in the order: FPC greater than MHM greater than SHM greater than or equal to SF. 5. Protease secretion from the pouches, assayed at pH 2-1, was in the order: MHM greater than SHM = FPC greater than SF. 6. The effect of dry matter (DM) intake and concentration on abomasal acidity was also studied in calves given diets which contained MHM (Expt 2). This diet was reconstituted at either 100 or 149 g DM/kg liquid diet and fed at either 32-5 or 49-0 g DM/kg live weight 0-75 per d. Samples of abomasal digesta were collected as in Expt 1. 7. A high intake of DM at a low DM concentration resulted in low acidity of the digesta in the first 3 h after feeding, which suggested a dilution effect. Comparison of two diets of different DM concentration, which were fed in the same volume of liquid, indicated that the greater the DM intake, the greater was the amount of acid secreted. 8. It is concluded that the protein sources varied in their ability to stimulate abomasal acid and protease secretion and it is suggested that this may relate to calf performance. | Milk-substitute diet composition and abomasal secretion in the calf. 1. The effect of different protein sources in milk-substitute diets on abomasal acidity and proteolytic activity was studied in Friesian calves, aged 20-58 d (Expt 1). The diets contained 'mildly' preheated, spray-dried skim-milk powder (MHM), severely preheated, spray-dried skim-milk powder (SHM), fish-protein concentrate (FPC) or solvent-extracted soya-bean flour (SF) as the main protein source. 2. Gastric juice was collected from abomasal pouches before feeding and at 15 min intervals for 8 h after the morning feed. Samples of digesta were obtained from the abomasum at 1 h intervals during the same period. 3. Digesta pH was lower and titratable acidity higher 0-3 after giving the diet containing MHM than when any of the other three diets was given. 3. Acid secretion from the pouches for the different diets was in the order: FPC greater than MHM greater than SHM greater than or equal to SF. 5. Protease secretion from the pouches, assayed at pH 2-1, was in the order: MHM greater than SHM = FPC greater than SF. 6. The effect of dry matter (DM) intake and concentration on abomasal acidity was also studied in calves given diets which contained MHM (Expt 2). This diet was reconstituted at either 100 or 149 g DM/kg liquid diet and fed at either 32-5 or 49-0 g DM/kg live weight 0-75 per d. Samples of abomasal digesta were collected as in Expt 1. 7. A high intake of DM at a low DM concentration resulted in low acidity of the digesta in the first 3 h after feeding, which suggested a dilution effect. Comparison of two diets of different DM concentration, which were fed in the same volume of liquid, indicated that the greater the DM intake, the greater was the amount of acid secreted. 8. It is concluded that the protein sources varied in their ability to stimulate abomasal acid and protease secretion and it is suggested that this may relate to calf performance. | [
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|
PMID:12784 | Studies on lipid digestion in the preruminant calf. The source of lipolytic activity in the abomasum. | 1. Lipolytic and proteolytic activities and pH values were determined in secretions collected from innervated abomasal pouches and in abomasal contents from preruminant calves given liquid diets. 2. No lipolytic activity was detected in pouch secretions collected during 1 h after feeding, though lipolytic activity was present in abomasal contents; pepsin (EC 3.4.23.1) and renin (EC 3.4.23.4) were present in both pouch secretions and abomasal contents. The pH values of pouch secretions ranged from 1-2 to 1-8 and those of abomasal contents from 4-2 to 5-9. 3. When diet was placed directly into the abomasal pouch soon after feeding, the pH values of pouch and abomasal contents decreased similarly (i.e. from 6-3 to approximately 5). Protease activity (U/ml) of pouch contents ranged from 0-1 to 0-8 and that of abomasal contents from 0-1 to 0-2. No lipolytic activity was detected in pouch contents, though abomasal contents contained 0-6 to 1-2 U/ml and when the diet contained milk-fat as the dietary fat source considerable lipolysis of triglycerides containing shorter-chain fatty acids was found. 4. It is concluded that there is no significant secretion of lipolytic enzymes by the fundal mucosa and that the lipolysis of triglycerides in the abomasum of the preruminant calf is due predominantly to a lipolytic enzyme in saliva. | Studies on lipid digestion in the preruminant calf. The source of lipolytic activity in the abomasum. 1. Lipolytic and proteolytic activities and pH values were determined in secretions collected from innervated abomasal pouches and in abomasal contents from preruminant calves given liquid diets. 2. No lipolytic activity was detected in pouch secretions collected during 1 h after feeding, though lipolytic activity was present in abomasal contents; pepsin (EC 3.4.23.1) and renin (EC 3.4.23.4) were present in both pouch secretions and abomasal contents. The pH values of pouch secretions ranged from 1-2 to 1-8 and those of abomasal contents from 4-2 to 5-9. 3. When diet was placed directly into the abomasal pouch soon after feeding, the pH values of pouch and abomasal contents decreased similarly (i.e. from 6-3 to approximately 5). Protease activity (U/ml) of pouch contents ranged from 0-1 to 0-8 and that of abomasal contents from 0-1 to 0-2. No lipolytic activity was detected in pouch contents, though abomasal contents contained 0-6 to 1-2 U/ml and when the diet contained milk-fat as the dietary fat source considerable lipolysis of triglycerides containing shorter-chain fatty acids was found. 4. It is concluded that there is no significant secretion of lipolytic enzymes by the fundal mucosa and that the lipolysis of triglycerides in the abomasum of the preruminant calf is due predominantly to a lipolytic enzyme in saliva. | [
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|
PMID:12785 | Studies on digestion and absorption in the intestines of growing pigs. Measurements of the flow of digesta and pH. | 1. Thirty-five pigs were fitted with single re-entrant cannulas in either the duodenum, jejunum or ileum. A further twenty-four pigs were used in a conventional digestibility trial. 2. Methods for collecting, sampling and returning digesta were developed. 3. A 'practical-type' diet and two purfied diets were used, fed twice daily. 4. Flow and pH of digesta were measured hourly in the duodenum and jejunum, and every 6 h in the ileum. 5. In the duodenum and jejunum there were clear flow responses to feeding, while such an effect was not found in the ileum where the flow-rate was much lower and more uniform than in the former sites. 6. In the duodenum and jejunum, and within 6 h periods in the ileum, there was considerable variation in the flow-rate between different pigs within each hour but there was less variation in pH. 7. The pattern of flow in the duodenum and jejunum was similar for each of the diets but the total flow and the average pH in 24 h differed significantly between diets. There were more digesta of a lower pH from the 'practical-type' diet than the purified diets. 8. The pH in the duodenum was highest after feeding and decreased with increasing time after feeding. In the jejunum and ileum the pH-varied over a much smaller range than in the duodenum. 9. Collections for 6 h periods appeared to be insufficiently long to predict the values obtained in 24 h collections with reasonable accuracy. | Studies on digestion and absorption in the intestines of growing pigs. Measurements of the flow of digesta and pH. 1. Thirty-five pigs were fitted with single re-entrant cannulas in either the duodenum, jejunum or ileum. A further twenty-four pigs were used in a conventional digestibility trial. 2. Methods for collecting, sampling and returning digesta were developed. 3. A 'practical-type' diet and two purfied diets were used, fed twice daily. 4. Flow and pH of digesta were measured hourly in the duodenum and jejunum, and every 6 h in the ileum. 5. In the duodenum and jejunum there were clear flow responses to feeding, while such an effect was not found in the ileum where the flow-rate was much lower and more uniform than in the former sites. 6. In the duodenum and jejunum, and within 6 h periods in the ileum, there was considerable variation in the flow-rate between different pigs within each hour but there was less variation in pH. 7. The pattern of flow in the duodenum and jejunum was similar for each of the diets but the total flow and the average pH in 24 h differed significantly between diets. There were more digesta of a lower pH from the 'practical-type' diet than the purified diets. 8. The pH in the duodenum was highest after feeding and decreased with increasing time after feeding. In the jejunum and ileum the pH-varied over a much smaller range than in the duodenum. 9. Collections for 6 h periods appeared to be insufficiently long to predict the values obtained in 24 h collections with reasonable accuracy. | [
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|
PMID:12787 | Proton-dependent dissociation equilibrium of hemoglobin. 1. A 700-nanometer light-scattering study on horse methemoglobin in the pH range 4.8 to 7.2. | The effect of proton concentration upon the subunit dissociation of horse methemoglobin has been investigated at two ionic strengths by light scattering photometry at 700 nm. Differential refractometry revealed a slight but systematic decrease of the specific refractive index increment with decreasing protein concentration for solutions in dialytic equilibrium with the solvent. In the pH range 4.8-7.2 the dissociation can be described by a simple equilibrium between tetramers and dimers. The dissociation constant Kd of the met derivative is found to be very similar to those of the O2- and CO-ligated states. From the slope of a plot of log Kd vs. pH, the number of protons bound is n = 1.3 +/- 0.1 resulting from an increase in the pK values of two groups upon dissociation. These two groups must be identical because the dissociation is symmetrical. | Proton-dependent dissociation equilibrium of hemoglobin. 1. A 700-nanometer light-scattering study on horse methemoglobin in the pH range 4.8 to 7.2. The effect of proton concentration upon the subunit dissociation of horse methemoglobin has been investigated at two ionic strengths by light scattering photometry at 700 nm. Differential refractometry revealed a slight but systematic decrease of the specific refractive index increment with decreasing protein concentration for solutions in dialytic equilibrium with the solvent. In the pH range 4.8-7.2 the dissociation can be described by a simple equilibrium between tetramers and dimers. The dissociation constant Kd of the met derivative is found to be very similar to those of the O2- and CO-ligated states. From the slope of a plot of log Kd vs. pH, the number of protons bound is n = 1.3 +/- 0.1 resulting from an increase in the pK values of two groups upon dissociation. These two groups must be identical because the dissociation is symmetrical. | [
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|
PMID:12788 | Proton-dependent dissociation equilibrium of hemoglobin. 2. Surface pressure measurements in monolayers of horse hemoglobin (III). | The molecular weight of hemoglobin (III) in monolayers on aqueous subsolutions has been determined by measuring the surface pressure as a function of the protein surface concentration. The dissociation equilibrium between tetrameric and dimeric hemoglobin (III) was determined for spread as well as adsorbed monolayers. The results were compared with analogous measurements in solution. It was found that the numerical value and the pH dependence of the dissociation constant were similar both in the bulk and in the surface phase of the solution. From these findings it was concluded that the native conformation of hemoglobin (III) is retained after adsorption at aqueous surface. | Proton-dependent dissociation equilibrium of hemoglobin. 2. Surface pressure measurements in monolayers of horse hemoglobin (III). The molecular weight of hemoglobin (III) in monolayers on aqueous subsolutions has been determined by measuring the surface pressure as a function of the protein surface concentration. The dissociation equilibrium between tetrameric and dimeric hemoglobin (III) was determined for spread as well as adsorbed monolayers. The results were compared with analogous measurements in solution. It was found that the numerical value and the pH dependence of the dissociation constant were similar both in the bulk and in the surface phase of the solution. From these findings it was concluded that the native conformation of hemoglobin (III) is retained after adsorption at aqueous surface. | [
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|
PMID:12789 | Conformational characteristics of luliberin. Circular dichroism and fluorescence studies. | By circular dichroism and fluorescence spectroscopy, the conformation of luliberin (luteinizing hormone-releasing hormone) has been investigated under various conditions of pH and solvents. Several structural parameters have been defined which seem predominant for the maintenance of the hormone in some privileged conformation(s). Formation of an intramolecular hydrogen bond between CO (His) and NH (Ser) seems likely when dissolving the hormone in organic solvent such as dioxane. Energy transfer has been demonstrated between Tyr and Trp residues. Calculation of the energy-transfer efficiency at different pH's allowed us to estimate in the range of 10 A the distance which separates these residues. Evidence is also provided for a charge-transfer interaction between protonated histidine and tryptophan. These data suggest that, when luliberin has organized structure (under appropriate surrounding conditions), its conformational pattern would resemble that of beta-turn structure in which a beta bend would exist at the level of the aromatic residues. | Conformational characteristics of luliberin. Circular dichroism and fluorescence studies. By circular dichroism and fluorescence spectroscopy, the conformation of luliberin (luteinizing hormone-releasing hormone) has been investigated under various conditions of pH and solvents. Several structural parameters have been defined which seem predominant for the maintenance of the hormone in some privileged conformation(s). Formation of an intramolecular hydrogen bond between CO (His) and NH (Ser) seems likely when dissolving the hormone in organic solvent such as dioxane. Energy transfer has been demonstrated between Tyr and Trp residues. Calculation of the energy-transfer efficiency at different pH's allowed us to estimate in the range of 10 A the distance which separates these residues. Evidence is also provided for a charge-transfer interaction between protonated histidine and tryptophan. These data suggest that, when luliberin has organized structure (under appropriate surrounding conditions), its conformational pattern would resemble that of beta-turn structure in which a beta bend would exist at the level of the aromatic residues. | [
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|
PMID:12790 | Conformational characteristics of luliberin. Luminescence properties at liquid-nitrogen temperature. | The luminescence properties (fluorescence and phosphorescence) of luliberin have been investigated at liquid-nitrogen temperature (77 K) in 50% ethylene glycolaqueous buffer at various pH's. Calculation of the energy-transfer efficiency between Trp and Tyr residues leads to an evaluation of the distance separating these residues. In alkaline medium, when tyrosine is ionized, a 100% transfer efficiency occurs from Trp to Tyr- at the singlet level and also from Tyr- to Trp at the triplet level indicating that the TRP-Tyr distance is less than about 5A. When luliberin is at pH 7.8 (or 4.5), transfer efficiency from Tyr to Trp at the singlet level is 85-90% which should correspond to a distance between Trp and Tyr of about 10-12 A. These results are discussed with respect to the role played by aromatic amino acids both in the hormone conformation and in the hormone biological potency. Moreover, comparison with the data obtained from fluorescence or circular dichroism studies at room temperature allows us to deduce some characteristics of luliberin conformation. Structure-activity relationships in the aromatic region of luliberin are also discussed. | Conformational characteristics of luliberin. Luminescence properties at liquid-nitrogen temperature. The luminescence properties (fluorescence and phosphorescence) of luliberin have been investigated at liquid-nitrogen temperature (77 K) in 50% ethylene glycolaqueous buffer at various pH's. Calculation of the energy-transfer efficiency between Trp and Tyr residues leads to an evaluation of the distance separating these residues. In alkaline medium, when tyrosine is ionized, a 100% transfer efficiency occurs from Trp to Tyr- at the singlet level and also from Tyr- to Trp at the triplet level indicating that the TRP-Tyr distance is less than about 5A. When luliberin is at pH 7.8 (or 4.5), transfer efficiency from Tyr to Trp at the singlet level is 85-90% which should correspond to a distance between Trp and Tyr of about 10-12 A. These results are discussed with respect to the role played by aromatic amino acids both in the hormone conformation and in the hormone biological potency. Moreover, comparison with the data obtained from fluorescence or circular dichroism studies at room temperature allows us to deduce some characteristics of luliberin conformation. Structure-activity relationships in the aromatic region of luliberin are also discussed. | [
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|
PMID:12791 | Purification of adenovirus messenger ribonucleic acid by an aqueous polymer two-phase system. | An aqueous polymer phase system containing 6.3% (w/w) dextran and 3.5% (w/w) poly(ethylene glycol) in 10 mM phosphate buffer (pH 8.0) was developed to select RNA-DNA hybrids from unhybridized RNA. The top phase of this phase system, which contains DNA and the RNA-DNA hybrids, can be used to purify adenovirus messenger RNA both early and late in the infectious cycle. The hybrids can be melted by heat in the top phase and the messenger RNA selected by oligo(dT)cellulose chromatography whereupon the polymers and the DNA percolate and the polyadenylated messenger RNA absorb to the column. The isolated messenger RNA appears to be almost quantitatively recovered at a purity from 70 to 90% depending on the concentration of the specific messenger RNA in the starting material. Early and late viral messenger RNA were selected on the complementary strands of adenovirus DNA according to this procedure. | Purification of adenovirus messenger ribonucleic acid by an aqueous polymer two-phase system. An aqueous polymer phase system containing 6.3% (w/w) dextran and 3.5% (w/w) poly(ethylene glycol) in 10 mM phosphate buffer (pH 8.0) was developed to select RNA-DNA hybrids from unhybridized RNA. The top phase of this phase system, which contains DNA and the RNA-DNA hybrids, can be used to purify adenovirus messenger RNA both early and late in the infectious cycle. The hybrids can be melted by heat in the top phase and the messenger RNA selected by oligo(dT)cellulose chromatography whereupon the polymers and the DNA percolate and the polyadenylated messenger RNA absorb to the column. The isolated messenger RNA appears to be almost quantitatively recovered at a purity from 70 to 90% depending on the concentration of the specific messenger RNA in the starting material. Early and late viral messenger RNA were selected on the complementary strands of adenovirus DNA according to this procedure. | [
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|
PMID:12792 | Intermediate states of actomyosin adenosine triphosphatase. | The early kinetic steps of actomyosin subfragment 1 (acto-S1) adenosine triphosphatase have been investigated by simultaneous monitoring of fluorescence and light scattering and also by observation of the time course of the production of phosphate. The results show that fluorescence enhancement occurs after the dissociation of actomyosin and that the rate of enhancement is similar to the maximum rate of enhancement for S1 alone, under similar conditions of pH and temperature. The maximum rate of the phosphate burst for acto S1 is also approximately the same as that for S1 alone. The maximum rates for fluorescence enhancement or phosphate formation are reached at much lower adenosine triphosphate concentrations for acto-S1 than for S1. An extension of the actomyosin scheme is presented which accounts for these results. | Intermediate states of actomyosin adenosine triphosphatase. The early kinetic steps of actomyosin subfragment 1 (acto-S1) adenosine triphosphatase have been investigated by simultaneous monitoring of fluorescence and light scattering and also by observation of the time course of the production of phosphate. The results show that fluorescence enhancement occurs after the dissociation of actomyosin and that the rate of enhancement is similar to the maximum rate of enhancement for S1 alone, under similar conditions of pH and temperature. The maximum rate of the phosphate burst for acto S1 is also approximately the same as that for S1 alone. The maximum rates for fluorescence enhancement or phosphate formation are reached at much lower adenosine triphosphate concentrations for acto-S1 than for S1. An extension of the actomyosin scheme is presented which accounts for these results. | [
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|
PMID:12793 | Energetics and mechanism of actomyosin adenosine triphosphatase. | Rate constants were determined for the reaction of actin with subfragment 1 (S1), S1-product complex, heavy meromyosin (HMM), and HMM-products complex for a range of temperatures, pH's, and ionic strengths. For actin concentrations up to 10 muM, the rate of reassociation of the product intermediate was equal to the rate of actomyosin subfragment 1 (acto-S1) or acto-HMM adenosine triphosphatase (ATPase). Therefore, under these conditions, the only important pathway for adenosine triphosphate hydrolysis is through the dissociation and recombination of S1 or HMM. The apparent rate constants for the association of S1 and S1-product with actin showed a similar large ionic strength dependence. The S1-product reaction had a large temperature dependence paralleling the rate of acto-S1 ATPase, while the reaction with S1 had a much smaller variation with temperature. The low value of the rate constant for the S1-product reaction and its relationship to the s1 areaction suggests that the apparent rate constant does not measure a simple second-order reaction. A plausible mechanism is a rapid equilibrium for the binding step, followed by a transition (product release) which increases the association constant. A refractory state could also reduce the apparent rate constant of recombination. An approximate assignment of equilibrium constants for the acto-S1 ATPase reaction was made based on the interpretation of the present evidence and equilibrium constnats for the S1 ATPase. | Energetics and mechanism of actomyosin adenosine triphosphatase. Rate constants were determined for the reaction of actin with subfragment 1 (S1), S1-product complex, heavy meromyosin (HMM), and HMM-products complex for a range of temperatures, pH's, and ionic strengths. For actin concentrations up to 10 muM, the rate of reassociation of the product intermediate was equal to the rate of actomyosin subfragment 1 (acto-S1) or acto-HMM adenosine triphosphatase (ATPase). Therefore, under these conditions, the only important pathway for adenosine triphosphate hydrolysis is through the dissociation and recombination of S1 or HMM. The apparent rate constants for the association of S1 and S1-product with actin showed a similar large ionic strength dependence. The S1-product reaction had a large temperature dependence paralleling the rate of acto-S1 ATPase, while the reaction with S1 had a much smaller variation with temperature. The low value of the rate constant for the S1-product reaction and its relationship to the s1 areaction suggests that the apparent rate constant does not measure a simple second-order reaction. A plausible mechanism is a rapid equilibrium for the binding step, followed by a transition (product release) which increases the association constant. A refractory state could also reduce the apparent rate constant of recombination. An approximate assignment of equilibrium constants for the acto-S1 ATPase reaction was made based on the interpretation of the present evidence and equilibrium constnats for the S1 ATPase. | [
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|
PMID:12794 | Relaxation spectra of yeast hexokinases. Isomerization of the enzyme. | Yeast hexokinase isozymes P1 and P11 exhibit a pH dependent, rapid relaxation process at 15 degrees C at enzyme concentrations of 100-474 muM and over a pH range of 6-8. The process was detected by equilibrium temperature jump spectroscopy using the indicator probe phenol red. The value of 1/tau varies from about 6 ms-1 at pH 8 for both isozymes to 50 ms-1 for P1 and 85 ms-1 for P11 at pH 6. The data are consistent with a mechanism involving an enzyme isomerization coupled to an ionization. The forward rate constant for the isomerization of the proposed mechanism varies between 3 and 7 ms-1; the ratio of the reverse rate constant to the ionization Ka is between 0.5 and 2 X 10(11) M-1 S-1; the estimated pKa varies between 5.5 and 6.1. The ranges of values in rate constants and pKa represent variations observed between preparations of the same isozyme and between isozymes. The isomerization rate is at least 50 times faster than catalysis under all conditions and the pKa is lower than that controlling activity. The rate of isomerization is unchanged by addition of sugar and nucleotide ligands, but the amplitude of the process is perturbed. These data imply that isomerizing and ionizing forms are sensitive to events at the active site. These equilibria between forms of hexokinase are fast enough, and have the right properties, to be important to the mechanism and regulation of the enzyme. | Relaxation spectra of yeast hexokinases. Isomerization of the enzyme. Yeast hexokinase isozymes P1 and P11 exhibit a pH dependent, rapid relaxation process at 15 degrees C at enzyme concentrations of 100-474 muM and over a pH range of 6-8. The process was detected by equilibrium temperature jump spectroscopy using the indicator probe phenol red. The value of 1/tau varies from about 6 ms-1 at pH 8 for both isozymes to 50 ms-1 for P1 and 85 ms-1 for P11 at pH 6. The data are consistent with a mechanism involving an enzyme isomerization coupled to an ionization. The forward rate constant for the isomerization of the proposed mechanism varies between 3 and 7 ms-1; the ratio of the reverse rate constant to the ionization Ka is between 0.5 and 2 X 10(11) M-1 S-1; the estimated pKa varies between 5.5 and 6.1. The ranges of values in rate constants and pKa represent variations observed between preparations of the same isozyme and between isozymes. The isomerization rate is at least 50 times faster than catalysis under all conditions and the pKa is lower than that controlling activity. The rate of isomerization is unchanged by addition of sugar and nucleotide ligands, but the amplitude of the process is perturbed. These data imply that isomerizing and ionizing forms are sensitive to events at the active site. These equilibria between forms of hexokinase are fast enough, and have the right properties, to be important to the mechanism and regulation of the enzyme. | [
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|
PMID:12795 | Effect of alcohols on the structure and function of D-amino-acid oxidase. | The absorption spectrum of D-amino-acid oxidase (D-amino-acid:oxygen oxidoreductase (deaminating), EC 1.4.3.3) was significantly perturbed by various alcohols; typical fine structures were observed in the visible absorption bands, accompanied by blue shifts of the peaks. Both fluorescence intensity and fluorescence polarization were increased upon the addition of alcohols, indicating that the coenzyme is not liberated from the apoenzyme but the hydrophobicity of the environment of the enzyme-bound flavin is increased. Upon the addition of alcohols, the circular dichroism of the enzyme was markedly modified in the visible and near-ultraviolet regions, while that of the apoenzyme in the near- and far-ultraviolet regions was scarcely modified, indicating a change in the interaction between the flavin coenzyme and protein. Both the apparent maximal velocity and the apparent Michaelis constant of the enzyme were increased by the addition of alcohols. The presence of alcohols tends to dissociate the dimer of this enzyme into the monomer, but the dissociation does not fully explain the increase in the maximal velocity of the enzyme by alcohols, because the increase in the maximal velocity caused by alcohols is larger than that expected from the dissociation. Since the rate of formation of the purple intermediate was decreased by alcohols in both the dimer and the monomer, the increase in the maximal velocity could be ascribed to an increase in the rate of dissociation of the enzyme-product complex. This increase could be ascribed to the protein conformational change, which is probably provoked by combination of alcohols with the enzyme at a locus other than that for substrate binding. | Effect of alcohols on the structure and function of D-amino-acid oxidase. The absorption spectrum of D-amino-acid oxidase (D-amino-acid:oxygen oxidoreductase (deaminating), EC 1.4.3.3) was significantly perturbed by various alcohols; typical fine structures were observed in the visible absorption bands, accompanied by blue shifts of the peaks. Both fluorescence intensity and fluorescence polarization were increased upon the addition of alcohols, indicating that the coenzyme is not liberated from the apoenzyme but the hydrophobicity of the environment of the enzyme-bound flavin is increased. Upon the addition of alcohols, the circular dichroism of the enzyme was markedly modified in the visible and near-ultraviolet regions, while that of the apoenzyme in the near- and far-ultraviolet regions was scarcely modified, indicating a change in the interaction between the flavin coenzyme and protein. Both the apparent maximal velocity and the apparent Michaelis constant of the enzyme were increased by the addition of alcohols. The presence of alcohols tends to dissociate the dimer of this enzyme into the monomer, but the dissociation does not fully explain the increase in the maximal velocity of the enzyme by alcohols, because the increase in the maximal velocity caused by alcohols is larger than that expected from the dissociation. Since the rate of formation of the purple intermediate was decreased by alcohols in both the dimer and the monomer, the increase in the maximal velocity could be ascribed to an increase in the rate of dissociation of the enzyme-product complex. This increase could be ascribed to the protein conformational change, which is probably provoked by combination of alcohols with the enzyme at a locus other than that for substrate binding. | [
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|
PMID:12796 | S-adenosylmethionine: protein-arginine methyltransferase. Purification and mechanism of the enzyme. | Protein methylase I (S-adenosylmethionine: protein-arginine methyltransferase, EC 2.1.1.23) has been purified from calf brain approximately 120-fold with a 14% yield. The final preparation is completely free of any other protein-specific methyltransferases and endogenous substrate protein. The enzyme has an optimum pH of 7.2 and pI value of 5.1. The Km values for S-adenosyl-L-methionine, histone H4, and an ancephalitogenic basic protein are 7.6 X 10(-6), 2.5 X 10(-5), and 7.1 X 10(-5) M, respectively, and the Ki value for S-adenosyl-L-homocysteine is 2.62 X 10(-6) M. The enzyme is highly specific for the arginine residues of protein, and the end products after hydrolysis of the methylated protein are NG,NG-di(asymmetric), NG,N'G-di(symmetric), and NG-monomethylarginine. The ratio of [14C]methyl incorporation into these derivatives by enzyme preparation at varying stages of purification remains unchanged at 40:5:55, strongly indicating that a single enzyme is involved in the synthesis of the three arginine derivatives. The kinetic mechanism of the protein methylase I reaction was studied with the purified enzyme. Initial velocity patterns converging at a point on the extended axis of abscissas were obtained with either histone H4 or S-adenosyl-L-methionine as the varied substrate. Product inhibition by S-adenosyl-L-homocysteine with S-adenosyl-L-methionine as the varied substrate was competitive regardless of whether or not the enzyme was saturated with histone H4. On the other hand, when histone H4 is the variable substrate, noncompetitive inhibition was obtained with S-adenosyl-L-homocysteine under conditions where the enzyme is not saturated with the other substrate, S-adenosyl-L-methionine. These results suggest that the mechanism of the protein methylase I reaction is a Sequential Ordered Bi Bi mechanism with S-adenosyl-L-methionine as the first substrate, histone H4 as the second substrate, methylated histone H4 as the first product, and S-adenosyl-L-homocysteine as the second product released. | S-adenosylmethionine: protein-arginine methyltransferase. Purification and mechanism of the enzyme. Protein methylase I (S-adenosylmethionine: protein-arginine methyltransferase, EC 2.1.1.23) has been purified from calf brain approximately 120-fold with a 14% yield. The final preparation is completely free of any other protein-specific methyltransferases and endogenous substrate protein. The enzyme has an optimum pH of 7.2 and pI value of 5.1. The Km values for S-adenosyl-L-methionine, histone H4, and an ancephalitogenic basic protein are 7.6 X 10(-6), 2.5 X 10(-5), and 7.1 X 10(-5) M, respectively, and the Ki value for S-adenosyl-L-homocysteine is 2.62 X 10(-6) M. The enzyme is highly specific for the arginine residues of protein, and the end products after hydrolysis of the methylated protein are NG,NG-di(asymmetric), NG,N'G-di(symmetric), and NG-monomethylarginine. The ratio of [14C]methyl incorporation into these derivatives by enzyme preparation at varying stages of purification remains unchanged at 40:5:55, strongly indicating that a single enzyme is involved in the synthesis of the three arginine derivatives. The kinetic mechanism of the protein methylase I reaction was studied with the purified enzyme. Initial velocity patterns converging at a point on the extended axis of abscissas were obtained with either histone H4 or S-adenosyl-L-methionine as the varied substrate. Product inhibition by S-adenosyl-L-homocysteine with S-adenosyl-L-methionine as the varied substrate was competitive regardless of whether or not the enzyme was saturated with histone H4. On the other hand, when histone H4 is the variable substrate, noncompetitive inhibition was obtained with S-adenosyl-L-homocysteine under conditions where the enzyme is not saturated with the other substrate, S-adenosyl-L-methionine. These results suggest that the mechanism of the protein methylase I reaction is a Sequential Ordered Bi Bi mechanism with S-adenosyl-L-methionine as the first substrate, histone H4 as the second substrate, methylated histone H4 as the first product, and S-adenosyl-L-homocysteine as the second product released. | [
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|
PMID:12797 | Purification and properties of Renilla reniformis luciferase. | Luciferase from the anthozoan coelenterate Renilla reniformis (Renilla luciferin:oxygen 2-oxidoreductase (decarboxylating), EC 1.13.12.5.) catalyzes the bioluminescent oxidation of Renilla luciferin producing light (lambdaB 480 nm, QB 5.5%), oxyluciferin, and CO2 (Hori, K., Wampler, J.E., Matthews, J.C., and Cormier, M.J. (1973), Biochemistry 12, 4463). Using a combination of ion-exchange, molecular-sieve, sulfhydryl-exchange, and affinity chromatography, luciferase has been purified, approximately 12 000-fold with 24% recovery, to homogeneity as judged by analysis with disc and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, gel filtration, and ultracentrifugation. Renilla luciferase is active as a nearly spherical single polypeptide chain monomer of 3.5 X 10(4) daltons having a specific activity of 1.8 X 10(15) hp s-1 mg-1 and a turnover number of 111 mumol min-1 mumol-1 of enzyme. This enzyme has a high content of aromatic and hydrophobic amino acids such that it has an epsilon280nm 0.1% of 2.1 and an average hydrophobicity of 1200 cal residue-1. The high average hydrophobicity of luciferase, which places it among the more hydrophobic proteins reported, is believed to account, at least in part, for its tendency to self-associate forming inactive dimers and higher molecular weight species. | Purification and properties of Renilla reniformis luciferase. Luciferase from the anthozoan coelenterate Renilla reniformis (Renilla luciferin:oxygen 2-oxidoreductase (decarboxylating), EC 1.13.12.5.) catalyzes the bioluminescent oxidation of Renilla luciferin producing light (lambdaB 480 nm, QB 5.5%), oxyluciferin, and CO2 (Hori, K., Wampler, J.E., Matthews, J.C., and Cormier, M.J. (1973), Biochemistry 12, 4463). Using a combination of ion-exchange, molecular-sieve, sulfhydryl-exchange, and affinity chromatography, luciferase has been purified, approximately 12 000-fold with 24% recovery, to homogeneity as judged by analysis with disc and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, gel filtration, and ultracentrifugation. Renilla luciferase is active as a nearly spherical single polypeptide chain monomer of 3.5 X 10(4) daltons having a specific activity of 1.8 X 10(15) hp s-1 mg-1 and a turnover number of 111 mumol min-1 mumol-1 of enzyme. This enzyme has a high content of aromatic and hydrophobic amino acids such that it has an epsilon280nm 0.1% of 2.1 and an average hydrophobicity of 1200 cal residue-1. The high average hydrophobicity of luciferase, which places it among the more hydrophobic proteins reported, is believed to account, at least in part, for its tendency to self-associate forming inactive dimers and higher molecular weight species. | [
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PMID:12798 | Oxidation of spermidine and spermine in rat liver: purification and properties of polyamine oxidase. | A novel enzyme responsible for the oxidation of spermidine and spermine has been found in rat liver. Spermidine is shown to be degraded to putrescine and 3-aminopropionaldehyde, and spermine to be cleaved to spermidine and 3-aminopropionaldehyde. A single enzyme catalyzing both reactions and designated as polyamine oxidase has been purified 4000-fold to electrophoretic homogeneity. Polyamine oxidase appears to be a flavoprotein, containing flavin adenine dinucleotide (FAD) as a prosthetic group. Hydrogen peroxide is evolved in the reaction and no other electron acceptors except molecular oxygen have been found. The molecular weight of the enzyme was approximately 60 000 and the sedimentation coefficient 4.5 S. The enzyme appears to be a single polypeptide chain since no evidence for structural subunits was obtained. Polyamine oxidase was sensitive to sulfhydryl and carbonyl group reagents. The optimum pH value for the oxidation of polyamines was close to 10. The reaction velocities were enhanced by various aldehydes, especially certain aromatic aldehydes. Polyamine oxidase appears to be localized in peroxisomes of liver cells, although the existence of an isoenzyme in the cytosolic fraction was not definitively ruled out. No marked changes were observed in the activity of polyamine oxidase in rat liver after partial hepatectomy, carbon tetrachloride poisoning, and after treatment with growth hormone or thioacetamide, conditions which are known to alter profoundly the metabolism and accumulation of polyamines. | Oxidation of spermidine and spermine in rat liver: purification and properties of polyamine oxidase. A novel enzyme responsible for the oxidation of spermidine and spermine has been found in rat liver. Spermidine is shown to be degraded to putrescine and 3-aminopropionaldehyde, and spermine to be cleaved to spermidine and 3-aminopropionaldehyde. A single enzyme catalyzing both reactions and designated as polyamine oxidase has been purified 4000-fold to electrophoretic homogeneity. Polyamine oxidase appears to be a flavoprotein, containing flavin adenine dinucleotide (FAD) as a prosthetic group. Hydrogen peroxide is evolved in the reaction and no other electron acceptors except molecular oxygen have been found. The molecular weight of the enzyme was approximately 60 000 and the sedimentation coefficient 4.5 S. The enzyme appears to be a single polypeptide chain since no evidence for structural subunits was obtained. Polyamine oxidase was sensitive to sulfhydryl and carbonyl group reagents. The optimum pH value for the oxidation of polyamines was close to 10. The reaction velocities were enhanced by various aldehydes, especially certain aromatic aldehydes. Polyamine oxidase appears to be localized in peroxisomes of liver cells, although the existence of an isoenzyme in the cytosolic fraction was not definitively ruled out. No marked changes were observed in the activity of polyamine oxidase in rat liver after partial hepatectomy, carbon tetrachloride poisoning, and after treatment with growth hormone or thioacetamide, conditions which are known to alter profoundly the metabolism and accumulation of polyamines. | [
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|
PMID:12799 | Hydrolysis of chyle cholesterol esters with cell-free preparations of rat liver. | 1. The effect of pH on the hydrolysis of chylomicron and chylomicron remnant cholesterol ester with rat liver homogenate was examined. The hydrolysis had three pH optima, at pH 4.5, at pH 6.0-6.5 and at pH 8.5. At the two upper pH optima extensive cholesterol ester hydrolysis occurred without simultaneous degradation of the triacylglycerol portion. 2. Similarly, microsomes (at pH 6.5-8.0) and 100 000 X g supernatant (at pH 7.5-8.5) efficiently hydrolyzed the cholesterol ester but not the triacylglycerol of chylomicron remnants. 3. With the same substrate no enrichment of neutral cholesterol esterase activity was seen in isolated plasma membranes. 4. At pH 4.5 lysosomes efficiently hydrolyzed both the cholesterol ester and the triacylglycerol portion of chylomicron remnants. 5. Three conclusions are drawn: (a) the study provides evidence against the existence of a plasma membrane-bound enzyme-hydrolyzing chylomicron cholesterol ester before or during its penetration into the cell; (b) enzymes of the cell sap and possibly of the endoplasmic reticulum can degrade cholesterol ester of chylomicron remnants without preceeding hydrolysis of the triacylglycerol core; and (c) lysosomal enzymes can degrade both the cholesterol ester and the triacylglycerol portion of chylomicron remnants if these are taken up as whole particles by endocytosis. | Hydrolysis of chyle cholesterol esters with cell-free preparations of rat liver. 1. The effect of pH on the hydrolysis of chylomicron and chylomicron remnant cholesterol ester with rat liver homogenate was examined. The hydrolysis had three pH optima, at pH 4.5, at pH 6.0-6.5 and at pH 8.5. At the two upper pH optima extensive cholesterol ester hydrolysis occurred without simultaneous degradation of the triacylglycerol portion. 2. Similarly, microsomes (at pH 6.5-8.0) and 100 000 X g supernatant (at pH 7.5-8.5) efficiently hydrolyzed the cholesterol ester but not the triacylglycerol of chylomicron remnants. 3. With the same substrate no enrichment of neutral cholesterol esterase activity was seen in isolated plasma membranes. 4. At pH 4.5 lysosomes efficiently hydrolyzed both the cholesterol ester and the triacylglycerol portion of chylomicron remnants. 5. Three conclusions are drawn: (a) the study provides evidence against the existence of a plasma membrane-bound enzyme-hydrolyzing chylomicron cholesterol ester before or during its penetration into the cell; (b) enzymes of the cell sap and possibly of the endoplasmic reticulum can degrade cholesterol ester of chylomicron remnants without preceeding hydrolysis of the triacylglycerol core; and (c) lysosomal enzymes can degrade both the cholesterol ester and the triacylglycerol portion of chylomicron remnants if these are taken up as whole particles by endocytosis. | [
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|
PMID:12800 | Characterization of the acetyl-CoA synthetase of Acetobacter aceti. | The acetate activating system of Acetobacter aceti has been studied. The enzyme responsible, acetyl-CoA synthetase, has been purified about 500-fold from crude cell extracts and was approximately 85% pure as judged by polyacrylamide gel electrophoresis in sodium dodecyl sulphate. The purified enzyme showed optimal activity at pH 7.6 in both Tris-HCL and potassium phosphate buffers. In its purest form, the enzyme was stable at 4 degrees-C but denatured upon freezing. The Km values for CoA, ATP and acetate were found to be 0.104 mM, 0.36 mM and 0.25 mM respectively; propionate and acrylate were also activated by the enzyme but not butyrate, isobutyrate or valerate. GTP, UTP, CTP and ADP could not replace ATP in the reaction, and cysteine or pantetheine failed to replace CoA. The cationic requirements were studied and of the divalent cations tested, only Mn2+ could significantly replace Mg2+ in the reaction; K+ and NH4+ stimulated enzyme activity but inhibited at high concentrations; Na+ was a poor activator, but did not inhibit at higher concentrations. The effect of a number of glucose and other metabolites on enzyme activity has been tested. | Characterization of the acetyl-CoA synthetase of Acetobacter aceti. The acetate activating system of Acetobacter aceti has been studied. The enzyme responsible, acetyl-CoA synthetase, has been purified about 500-fold from crude cell extracts and was approximately 85% pure as judged by polyacrylamide gel electrophoresis in sodium dodecyl sulphate. The purified enzyme showed optimal activity at pH 7.6 in both Tris-HCL and potassium phosphate buffers. In its purest form, the enzyme was stable at 4 degrees-C but denatured upon freezing. The Km values for CoA, ATP and acetate were found to be 0.104 mM, 0.36 mM and 0.25 mM respectively; propionate and acrylate were also activated by the enzyme but not butyrate, isobutyrate or valerate. GTP, UTP, CTP and ADP could not replace ATP in the reaction, and cysteine or pantetheine failed to replace CoA. The cationic requirements were studied and of the divalent cations tested, only Mn2+ could significantly replace Mg2+ in the reaction; K+ and NH4+ stimulated enzyme activity but inhibited at high concentrations; Na+ was a poor activator, but did not inhibit at higher concentrations. The effect of a number of glucose and other metabolites on enzyme activity has been tested. | [
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|
PMID:12801 | Stabilization of an acetyl-coenzyme A carboxylase complex from Pseudomonas citronellolis. | Using stabilizing conditions the acetyl-CoA carboxylase (EC 6.4.1.2) of Pseudomonas citronellolis has been isolated as a complex containing four different polypeptide chains with molecular weights of 53 000, 36 000, 33 000 and 25 000. Evidence is presented to suggest that these polypeptide chains correspond to distinct biotin carboxylase, transcarboxylase and biotin carboxyl carrier protein subunits in analogy with similar subunits of Escherichia coli acetyl-CoA carboxylase, an unstable complex in vitro. | Stabilization of an acetyl-coenzyme A carboxylase complex from Pseudomonas citronellolis. Using stabilizing conditions the acetyl-CoA carboxylase (EC 6.4.1.2) of Pseudomonas citronellolis has been isolated as a complex containing four different polypeptide chains with molecular weights of 53 000, 36 000, 33 000 and 25 000. Evidence is presented to suggest that these polypeptide chains correspond to distinct biotin carboxylase, transcarboxylase and biotin carboxyl carrier protein subunits in analogy with similar subunits of Escherichia coli acetyl-CoA carboxylase, an unstable complex in vitro. | [
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|
PMID:12802 | Effect of sodium fluoride on glucose-6-phosphate dehydrogenase activity in the rat uterus. | Intrauterine administration of 50 mumol of NaF to the ovariectomized mature rat causes a 2--3-fold increase in the total uterine glucose-6-phosphate dehydrogenase activity within 24 h. The response is characterized by a 4--6 h lag with a maximum effect from 24 to 36 h after a single treatment. Uterine glucose-6-phosphate dehydrogenase activity continues to increase with daily administration of NaF through 4 days. The NaF-induced response is blocked by prior intrauterine administration of cycloheximide but not actinomycin D suggesting that the enzyme activity increases by a post-transcriptional effect of NaF on de novo enzyme synthesis. Direct measurement of the effect of NaF on the rate of incorporation of [14C] leucine into immunoprecipitable uterine glucose-6-phosphate dehydrogenase indicates that NaF causes a 9-fold increase in the rate of enzyme synthesis during the interval from 12 to 16 h after treatment. The half-life of the enzyme as measured by the rate of loss of [1-14C] glutamate from previously labeled utreine glucose-6-phosphate dehydrogenase is decreased from 27 to 10 h by NaF. The NaF response does not seem to be mediated by activation of uterine adenylyl cyclase since theophylline does not potentiate the response and since intrauterine application of cyclic AMP does not mimic the response. The increase in enzyme activity is preceded by an increase in the rate of utilization of the hexose monophosphate shunt pathway as determined by the ratio of the the rates of oxidation of [1-14C]glucose to [6-14C] glucose to CO2 by uterine slices in vitro. The action of NaF on this pathway most likely resutls from inhibition of the glycolytic enzyme, enolase, and increased pathway utilization may be the factor which controls enzyme synthesis. When given in combination with other known inducers of uterine glucose-6-phosphate dehydrogenase such as estradiol and NADP+, NaF acts synergistically. | Effect of sodium fluoride on glucose-6-phosphate dehydrogenase activity in the rat uterus. Intrauterine administration of 50 mumol of NaF to the ovariectomized mature rat causes a 2--3-fold increase in the total uterine glucose-6-phosphate dehydrogenase activity within 24 h. The response is characterized by a 4--6 h lag with a maximum effect from 24 to 36 h after a single treatment. Uterine glucose-6-phosphate dehydrogenase activity continues to increase with daily administration of NaF through 4 days. The NaF-induced response is blocked by prior intrauterine administration of cycloheximide but not actinomycin D suggesting that the enzyme activity increases by a post-transcriptional effect of NaF on de novo enzyme synthesis. Direct measurement of the effect of NaF on the rate of incorporation of [14C] leucine into immunoprecipitable uterine glucose-6-phosphate dehydrogenase indicates that NaF causes a 9-fold increase in the rate of enzyme synthesis during the interval from 12 to 16 h after treatment. The half-life of the enzyme as measured by the rate of loss of [1-14C] glutamate from previously labeled utreine glucose-6-phosphate dehydrogenase is decreased from 27 to 10 h by NaF. The NaF response does not seem to be mediated by activation of uterine adenylyl cyclase since theophylline does not potentiate the response and since intrauterine application of cyclic AMP does not mimic the response. The increase in enzyme activity is preceded by an increase in the rate of utilization of the hexose monophosphate shunt pathway as determined by the ratio of the the rates of oxidation of [1-14C]glucose to [6-14C] glucose to CO2 by uterine slices in vitro. The action of NaF on this pathway most likely resutls from inhibition of the glycolytic enzyme, enolase, and increased pathway utilization may be the factor which controls enzyme synthesis. When given in combination with other known inducers of uterine glucose-6-phosphate dehydrogenase such as estradiol and NADP+, NaF acts synergistically. | [
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|
PMID:12803 | Acid inactivation of short-lived rat liver enzymes. | The stabilities of nine rat liver cytosol enzymes were compared at a variety of pH values. The cytosol enzymes studied were (a) those with half-lives in vivo of 3 days or longer: lactate dehydrogenase, arginase, glyceraldehyde phosphate dehydrogenase and alanine aminotransferase, (b) those with half-lives in vivo shorter than 2 days; glucokinase, dihydroorotase, serine dehydratase and tyrosine aminotransferase and (c) catalase, which has an intermediate half-life of 2.5 days for the protein protion. All the enzymes were stable in vitro at neurtal and alkaline pH values. However, at acidic pH values (pH 4): the long-lived enzymes (a) were stable; the short-lived enzymes (b) were completely inactivated with one exception; and catalase was partially inactivated. Tyrosine aminotransferase was the exception in that it is a short-lived enzyme in vivo but stable under all conditions tested in vitro. The finding that long-lived enzymes are stable in an acid milieu and short-lived enzymes are generally unstable was only observed if certain ligands (NAD+, pyridoxal 5'-phosphate, Mn2+, amino acids) were added to the invitro system. Lysosomal extracts did not accelerate the rate of inactivation of any cytosol enzyme in acidic solutions. These results indicate that if degradation of intracellular enzymes occurs in lysosomes, acid inactivation and denaturation of enzymes may be the initial event in determining the functional half-lives of the enzymes in vivo. | Acid inactivation of short-lived rat liver enzymes. The stabilities of nine rat liver cytosol enzymes were compared at a variety of pH values. The cytosol enzymes studied were (a) those with half-lives in vivo of 3 days or longer: lactate dehydrogenase, arginase, glyceraldehyde phosphate dehydrogenase and alanine aminotransferase, (b) those with half-lives in vivo shorter than 2 days; glucokinase, dihydroorotase, serine dehydratase and tyrosine aminotransferase and (c) catalase, which has an intermediate half-life of 2.5 days for the protein protion. All the enzymes were stable in vitro at neurtal and alkaline pH values. However, at acidic pH values (pH 4): the long-lived enzymes (a) were stable; the short-lived enzymes (b) were completely inactivated with one exception; and catalase was partially inactivated. Tyrosine aminotransferase was the exception in that it is a short-lived enzyme in vivo but stable under all conditions tested in vitro. The finding that long-lived enzymes are stable in an acid milieu and short-lived enzymes are generally unstable was only observed if certain ligands (NAD+, pyridoxal 5'-phosphate, Mn2+, amino acids) were added to the invitro system. Lysosomal extracts did not accelerate the rate of inactivation of any cytosol enzyme in acidic solutions. These results indicate that if degradation of intracellular enzymes occurs in lysosomes, acid inactivation and denaturation of enzymes may be the initial event in determining the functional half-lives of the enzymes in vivo. | [
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PMID:12804 | Thermoplasma acidophilum: intracellular pH and potassium concentration. | Thermoplasma acidophilum is a free-living thermophilic mycoplasma. Although the organism lacks a cell wall, it can grow in medium as dilute as 66 mosM. The intracellular K+ concentration can be as low as 17 mM, but varies according to the osmolality of the culture medium. The internal pH can be measured by taking advantage of the fact that T. acidophilum undergoes lysis when the pH is adjusted to neutrality. Thus, by appropriate analysis of titration curves, it is possible to conclude that the internal pH is near 5.5. This result was confirmed by a second type of experiment in which the internal pH was analyzed by rupturing the cells in a French Pressure Cell. | Thermoplasma acidophilum: intracellular pH and potassium concentration. Thermoplasma acidophilum is a free-living thermophilic mycoplasma. Although the organism lacks a cell wall, it can grow in medium as dilute as 66 mosM. The intracellular K+ concentration can be as low as 17 mM, but varies according to the osmolality of the culture medium. The internal pH can be measured by taking advantage of the fact that T. acidophilum undergoes lysis when the pH is adjusted to neutrality. Thus, by appropriate analysis of titration curves, it is possible to conclude that the internal pH is near 5.5. This result was confirmed by a second type of experiment in which the internal pH was analyzed by rupturing the cells in a French Pressure Cell. | [
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|
PMID:12805 | Mechanism of the inhibitory effect of glyoxylate plus oxaloacetate and oxalomalate on the NADP-specific isocitrate dehydrogenase. | The effects of glyoxylate plus oxaloacetate and of oxalomalate on the NADP-linked isocitrate dehydrogenase (threo-DS-isocitrate:NADP+ oxidoreductase (decarboxylating, EC 1.1.1.42) from pig heart from been studied with steady state methods as well as with stopped flow technique. When equimolar mixtures of glyoxylate and oxaloacetate were premixed for different lengths of time prior to addition to the assay mixture, the extent of inhibition increased with the premixing time. The results indicated that the inhibition by glyoxylate plus oxaloacetate is caused by a compound formed in a reversible interaction between the two components. Glyoxylate plus oxaloacetate and oxalomalate affected the enzyme in at least three different ways. They inhibited the enzyme in a reaction competitive with regard to the substrate isocitrate. This inhibition needed a certain time to be fully expressed. The time lag could be eliminated by premixing of the enzyme and inhibitor with NADP plus metal ion. Secondly, if the enzyme is premixed with NADP plus metal ions, a time lag occurs before the reaction rate approaches a constant value after initiation of the reaction with isocitrate. The inhibitors were found to enhance this effect of NADP plus metal ions on the enzyme. Thirdly, it has previously been shown that the enzyme can be activated by metal complexing agents. Glyoxylate plus oxaloacetate as well as oxalomalate are able to form complexes with metal ions and were found to cause an initial activation of the enzyme under certain assay conditions. The controversy regarding the mechanism of action of the above inhibitors on the enzyme is probably due to the fact that they affect the enzyme in several different ways. | Mechanism of the inhibitory effect of glyoxylate plus oxaloacetate and oxalomalate on the NADP-specific isocitrate dehydrogenase. The effects of glyoxylate plus oxaloacetate and of oxalomalate on the NADP-linked isocitrate dehydrogenase (threo-DS-isocitrate:NADP+ oxidoreductase (decarboxylating, EC 1.1.1.42) from pig heart from been studied with steady state methods as well as with stopped flow technique. When equimolar mixtures of glyoxylate and oxaloacetate were premixed for different lengths of time prior to addition to the assay mixture, the extent of inhibition increased with the premixing time. The results indicated that the inhibition by glyoxylate plus oxaloacetate is caused by a compound formed in a reversible interaction between the two components. Glyoxylate plus oxaloacetate and oxalomalate affected the enzyme in at least three different ways. They inhibited the enzyme in a reaction competitive with regard to the substrate isocitrate. This inhibition needed a certain time to be fully expressed. The time lag could be eliminated by premixing of the enzyme and inhibitor with NADP plus metal ion. Secondly, if the enzyme is premixed with NADP plus metal ions, a time lag occurs before the reaction rate approaches a constant value after initiation of the reaction with isocitrate. The inhibitors were found to enhance this effect of NADP plus metal ions on the enzyme. Thirdly, it has previously been shown that the enzyme can be activated by metal complexing agents. Glyoxylate plus oxaloacetate as well as oxalomalate are able to form complexes with metal ions and were found to cause an initial activation of the enzyme under certain assay conditions. The controversy regarding the mechanism of action of the above inhibitors on the enzyme is probably due to the fact that they affect the enzyme in several different ways. | [
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PMID:12806 | Determination of the redox potential of deazariboflavin by equilibration with flavins. | The redox potential of deazariboflavin has been determined for pH values from 5.5 to 9.2 by equilibration with riboflavin and lumiflavin 3-acetate. The position of the equilibrium with riboflavin was measured spectrophotometrically and fluorimetrically; the equilibrium potential with lumiflavin 3-acetate was measured spectrophotometrically and potentiometrically. The Em7 for deazariboflavin was found to be--0.273 +/- 0.003 V against the standard hydrogen electrode. Equilibrium with flavodoxin at pH 9.5 and 10.0 was also used to determine the redox potential of deazariboflavin at high pH values. The pK of dihydrodeazariboflavin was found from the break in the potential vs. pH diagram and from spectrophotometric pH titration. The pK value obtained by both methods is 7.00 +/- 0.05. We found that borate, a product of the reducing agent borohydride, complexed with the ribityl sidechain of deazariboflavin, causing a shift in the pK for the reduced form to values of about 8. | Determination of the redox potential of deazariboflavin by equilibration with flavins. The redox potential of deazariboflavin has been determined for pH values from 5.5 to 9.2 by equilibration with riboflavin and lumiflavin 3-acetate. The position of the equilibrium with riboflavin was measured spectrophotometrically and fluorimetrically; the equilibrium potential with lumiflavin 3-acetate was measured spectrophotometrically and potentiometrically. The Em7 for deazariboflavin was found to be--0.273 +/- 0.003 V against the standard hydrogen electrode. Equilibrium with flavodoxin at pH 9.5 and 10.0 was also used to determine the redox potential of deazariboflavin at high pH values. The pK of dihydrodeazariboflavin was found from the break in the potential vs. pH diagram and from spectrophotometric pH titration. The pK value obtained by both methods is 7.00 +/- 0.05. We found that borate, a product of the reducing agent borohydride, complexed with the ribityl sidechain of deazariboflavin, causing a shift in the pK for the reduced form to values of about 8. | [
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|
PMID:12807 | Isolation, purification and characterization of bovine epidermal transglutaminase. | A crosslinking enzyme, epidermal transglutaminase, was isolated from soluble proteins of glabrous cow snout epidermis. This enzyme stabilized fibrin clots rendering them insoluble in 2% acetic acid. It also catalyzed the incorporation of the fluorescent amine, dansyl cadaverine, into casein. Epidermal transglutaminase was purified by chromatography upon DEAE-Sephadex A-50, zone electrophoresis in Pevikon, and Sephadex G-200 gel permeation chromatography. The highly purified substance, which had a specific activity of 3267 amine-incorporating units/mg per h and a molecular weight of 55000, behaved as a single molecular species in the analytical ultracentrifuge. It had a sedimentation coefficient of 4.4 S and migrated as a gamma-globulin at pH 8.6; it displayed anomalous migration in polyacrylamide gels containing sodium dodecyl sulfate. The enzyme was dependent upon free calcium ions and a reduced sulfhydryl group for activity. The apparent Km for dansyl cadaverine was 1.2 - 10(-4) at pH 7.5. Monospecific antiserum to bovine epidermal transglutaminase precipitated with the enzyme in agar. The antiserum prevented fibrin crosslinking but enhanced incorporation of dansyl cadaverine into casein by the enzyme. The epidermal enzyme differed biochemically and immunochemically from bovine plasma transglutaminase (Factor XIII). | Isolation, purification and characterization of bovine epidermal transglutaminase. A crosslinking enzyme, epidermal transglutaminase, was isolated from soluble proteins of glabrous cow snout epidermis. This enzyme stabilized fibrin clots rendering them insoluble in 2% acetic acid. It also catalyzed the incorporation of the fluorescent amine, dansyl cadaverine, into casein. Epidermal transglutaminase was purified by chromatography upon DEAE-Sephadex A-50, zone electrophoresis in Pevikon, and Sephadex G-200 gel permeation chromatography. The highly purified substance, which had a specific activity of 3267 amine-incorporating units/mg per h and a molecular weight of 55000, behaved as a single molecular species in the analytical ultracentrifuge. It had a sedimentation coefficient of 4.4 S and migrated as a gamma-globulin at pH 8.6; it displayed anomalous migration in polyacrylamide gels containing sodium dodecyl sulfate. The enzyme was dependent upon free calcium ions and a reduced sulfhydryl group for activity. The apparent Km for dansyl cadaverine was 1.2 - 10(-4) at pH 7.5. Monospecific antiserum to bovine epidermal transglutaminase precipitated with the enzyme in agar. The antiserum prevented fibrin crosslinking but enhanced incorporation of dansyl cadaverine into casein by the enzyme. The epidermal enzyme differed biochemically and immunochemically from bovine plasma transglutaminase (Factor XIII). | [
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|
PMID:12808 | Molecular heterogeneity of rabbit heart phosphorylase kinase. | Phosphorylase kinase (ATP: phosphorylase-b phosphotransferase, EC 2.7.1.38) from rabbit heart, when submitted to electrophoresis on Pevikon, separates into two discrete peaks A and B. The two peaks have been analyzed using reelectrophoresis, chromatography on DEAE-cellulose, thermal stability, inactivation by EGTA (ethyleneglycol-bis(beta-aminoethyl ether)-N,N'-tetraacetic acid) and reaction with an anti-muscle phosphorylase kinase antiserum. It can be concluded that rabbit heart extracts contain two isozymes of phosphorylase kinase. The more negatively charged isozyme seems to be identical with the muscle enzyme. The other isozyme resembles the liver enzyme but differs from the major fraction of the latter by its charge. It is likely that there exist at least three molecular types of phosphorylase kinase. | Molecular heterogeneity of rabbit heart phosphorylase kinase. Phosphorylase kinase (ATP: phosphorylase-b phosphotransferase, EC 2.7.1.38) from rabbit heart, when submitted to electrophoresis on Pevikon, separates into two discrete peaks A and B. The two peaks have been analyzed using reelectrophoresis, chromatography on DEAE-cellulose, thermal stability, inactivation by EGTA (ethyleneglycol-bis(beta-aminoethyl ether)-N,N'-tetraacetic acid) and reaction with an anti-muscle phosphorylase kinase antiserum. It can be concluded that rabbit heart extracts contain two isozymes of phosphorylase kinase. The more negatively charged isozyme seems to be identical with the muscle enzyme. The other isozyme resembles the liver enzyme but differs from the major fraction of the latter by its charge. It is likely that there exist at least three molecular types of phosphorylase kinase. | [
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|
PMID:12809 | External yeast beta-fructosidase. Affinity labeling of the active site. | Conduritol-B-epoxide, a compound structurally related to the substrates of external yeast beta-fructosidase (beta-D-fructofuranoside fructohydrolase, EC 3.2.1.26), is an active-site directed inhibitor of this enzyme. The inactivation is irreversible and first-order with respect to time and inhibitor concentration. From the kinetic data obtained, it is concluded that one molecule of inhibitor reacts with one molecule of the enzyme causing inactivation. The inactivation is prevented by the presence of substrates. The pH-dependence of inactivation shows two dissociating groups in the enzyme with pKa values 3.05 and 6.8 being involved in the inactivation process. A carboxylate at the active site with pKa 3.05 is suggested to be the reactive group with conduritol-B-epoxide. | External yeast beta-fructosidase. Affinity labeling of the active site. Conduritol-B-epoxide, a compound structurally related to the substrates of external yeast beta-fructosidase (beta-D-fructofuranoside fructohydrolase, EC 3.2.1.26), is an active-site directed inhibitor of this enzyme. The inactivation is irreversible and first-order with respect to time and inhibitor concentration. From the kinetic data obtained, it is concluded that one molecule of inhibitor reacts with one molecule of the enzyme causing inactivation. The inactivation is prevented by the presence of substrates. The pH-dependence of inactivation shows two dissociating groups in the enzyme with pKa values 3.05 and 6.8 being involved in the inactivation process. A carboxylate at the active site with pKa 3.05 is suggested to be the reactive group with conduritol-B-epoxide. | [
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|
PMID:12810 | On the catalytic and binding sites of porcine enteropeptidase. | The active site of porcine enteropeptidase (EC 3.4.21.9) was investigated in order to characterize better both catalytic and binding sites. The participation of a serine and a histidine residue in the catalytic process was fully confirmed and the two residues were located on the light chain of the enzyme. The binding site was found to be composed of at least 2 subsites S1 and S2. The subsite S1 (similar to the trypsin-binding site) is responsible for the interactions with the small substrates of trypsin and the lysine side chain of trypsinogen, while subsite S2 (probably a cluster of lysines) is responsible for the interactions with the polyanionic sequence found in all trypsinogens. Binding of substrate by subsite S2 led to an increased efficiency of the catalytic site which can be correlated to the known high specificity of enteropeptidase. | On the catalytic and binding sites of porcine enteropeptidase. The active site of porcine enteropeptidase (EC 3.4.21.9) was investigated in order to characterize better both catalytic and binding sites. The participation of a serine and a histidine residue in the catalytic process was fully confirmed and the two residues were located on the light chain of the enzyme. The binding site was found to be composed of at least 2 subsites S1 and S2. The subsite S1 (similar to the trypsin-binding site) is responsible for the interactions with the small substrates of trypsin and the lysine side chain of trypsinogen, while subsite S2 (probably a cluster of lysines) is responsible for the interactions with the polyanionic sequence found in all trypsinogens. Binding of substrate by subsite S2 led to an increased efficiency of the catalytic site which can be correlated to the known high specificity of enteropeptidase. | [
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|
PMID:12811 | On the specificity of bovine spleen cathepsin B2. | The specificity of bovine spleen cathepsin B2 has been investigated by means of some natural oligo- and polypeptides, i.e. glucagon, melittin, insulin A and B chain, bradykinin, angiotensin I and II, oxytocin ACTH, clupein and salmin. The enzyme is primarily a carboxypeptidase which hydrolyzes peptide linkages of most amino acids common to proteins. In addition, cathepsin B2 displays amidase and esterase activity without requiring a free carboxyl group. The main pH optimum is between 4 and 5, in some cases higher. | On the specificity of bovine spleen cathepsin B2. The specificity of bovine spleen cathepsin B2 has been investigated by means of some natural oligo- and polypeptides, i.e. glucagon, melittin, insulin A and B chain, bradykinin, angiotensin I and II, oxytocin ACTH, clupein and salmin. The enzyme is primarily a carboxypeptidase which hydrolyzes peptide linkages of most amino acids common to proteins. In addition, cathepsin B2 displays amidase and esterase activity without requiring a free carboxyl group. The main pH optimum is between 4 and 5, in some cases higher. | [
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|
PMID:12812 | Activation of proenzyme of acidic protease from human seminal plasma. | The kinetics and the extent of the conversion of the proenzyme into the active acidic protease (EC 3.4.23.--) of human seminal plasma were dependent on acidic pH. Between pH 2 and 4, the initial rate of the activation was first-order with respect to the proenzyme. Between pH 4.5 and 5, the rate deviated from the first-order with an initial lag period which can be abolished by adding an excess amount of the acidic protease or pepsin. The extent of the activation was complete between pH 2 and 3 and became incomplete between pH 4 and 5. Addition of the acidic protease or pepsin did not alter the extent of the activation at the high pH values. According to the chromatographic profile on a Sephadex G-75 column, the activation products (namely active acidic protease and an activation peptide) obtained at pH 3 and those obtained at pH 4.5 were identical. The molecular weight of the activation peptide obtained at pH 3 was 6900; its amino acid composition was analyzed and compared with those of the proenzyme and the acidic protease. Remarkable similarity between the amino acid composition of the acidic protease and that of human pepsin was observed. In the presence of an excess amount of hemoglobin, the conversion of the proenzyme was self-activated and showed an initial lag period. Addition of acidic protease did not change the rate of self activation or the lag period. | Activation of proenzyme of acidic protease from human seminal plasma. The kinetics and the extent of the conversion of the proenzyme into the active acidic protease (EC 3.4.23.--) of human seminal plasma were dependent on acidic pH. Between pH 2 and 4, the initial rate of the activation was first-order with respect to the proenzyme. Between pH 4.5 and 5, the rate deviated from the first-order with an initial lag period which can be abolished by adding an excess amount of the acidic protease or pepsin. The extent of the activation was complete between pH 2 and 3 and became incomplete between pH 4 and 5. Addition of the acidic protease or pepsin did not alter the extent of the activation at the high pH values. According to the chromatographic profile on a Sephadex G-75 column, the activation products (namely active acidic protease and an activation peptide) obtained at pH 3 and those obtained at pH 4.5 were identical. The molecular weight of the activation peptide obtained at pH 3 was 6900; its amino acid composition was analyzed and compared with those of the proenzyme and the acidic protease. Remarkable similarity between the amino acid composition of the acidic protease and that of human pepsin was observed. In the presence of an excess amount of hemoglobin, the conversion of the proenzyme was self-activated and showed an initial lag period. Addition of acidic protease did not change the rate of self activation or the lag period. | [
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|
PMID:12813 | Delayed fluorescence from bacteriochlorophyll in Chromatium vinosum chromatophores. | Delayed fluorescence from bacteriochlorophyll in Chromatium vinosum chromatophores was studied at room temperature and under intermittent illuminations. The decay of delayed fluorescence was constituted of two components; a fast component decayed with a half time of about 8 ms, a slow one decayed in parallel with the reduction of photooxidized bacteriochlorophyll (P+) with a half time of 100-200 ms. The biphasic decay of delayed fluorescence indicated that a rapid equilibrium was established between the primary electron acceptor and the secondary acceptor. In the presence of o-phenanthroline, the time course of the decay of delayed fluorescence was identical with that of the reduction of P+ in reaction center-rich subchromatophore particles, although they did not necessarily coincide with each other in "intact" chromatophores. The intensity of the slow component was increased and the decay was accelerated at basic pH values. Reagents that dissipate the proton gradient across the chromatophore membranes such as carbonylcyanide m-chlorophenylhydrazone (CCCP) and nigericin accelerated the decay of the slow component. These effects are probably resulting from changes in internal pH of chromatophore vesicles. Reagents that dissipate the membrane potential such as CCCP and valinomycin decreased the intensity. | Delayed fluorescence from bacteriochlorophyll in Chromatium vinosum chromatophores. Delayed fluorescence from bacteriochlorophyll in Chromatium vinosum chromatophores was studied at room temperature and under intermittent illuminations. The decay of delayed fluorescence was constituted of two components; a fast component decayed with a half time of about 8 ms, a slow one decayed in parallel with the reduction of photooxidized bacteriochlorophyll (P+) with a half time of 100-200 ms. The biphasic decay of delayed fluorescence indicated that a rapid equilibrium was established between the primary electron acceptor and the secondary acceptor. In the presence of o-phenanthroline, the time course of the decay of delayed fluorescence was identical with that of the reduction of P+ in reaction center-rich subchromatophore particles, although they did not necessarily coincide with each other in "intact" chromatophores. The intensity of the slow component was increased and the decay was accelerated at basic pH values. Reagents that dissipate the proton gradient across the chromatophore membranes such as carbonylcyanide m-chlorophenylhydrazone (CCCP) and nigericin accelerated the decay of the slow component. These effects are probably resulting from changes in internal pH of chromatophore vesicles. Reagents that dissipate the membrane potential such as CCCP and valinomycin decreased the intensity. | [
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|
PMID:12814 | Proton electrochemical potential in steady state rat liver mitochondria. | Delta approximately muH has been determined in steady state mitochondria by measuring the magnitude of delta pH on the distribution of acetate and of deltapsi on the distribution of K+, tetraphenylphosphonium, Ca2+, Sr2+ and Mn2+. (1) The matrix concentration of divalent cations has been calculated from the total cation uptake, from the increase of matrix volume and from the ESR sextet signal of Mn(H2O)L2+. The [cat2+]i based on osmotic data is about five times higher than that based on ESR measurements. The [cat2+]i based on total uptake is much higher than that based on osmotic data at low cation/protein ratios. (2) In the presence of 10 mM acetate the maximal deltapsi on Ca2+ is about 130 mV and on Sr2+ is 95 mV. Deltapsi on Mn2+ is 91 or 109 mV, according to whether [cat2+-a)i is calculated from ESR or osmotic data. Under the same conditions, deltapH is about 60 mV. Hence delta approximately muH on divalent cations is between 151 and 190 mV. (3) Deltapsi on K+, in valinomycin treated mitochondria with 10 mM acetate or 2 mM Pi, drops from 200 mV, at low [K+]0 to almost zero parallel to the increase of [K+]0. DeltapH is 30 mV at low [K+]0 and about 42 mV at 600 muM K+. Hence delta approximately muH drops from 22m mV lower values with the increase of [K+]0. (4) Maximal deltapsi on triphenylmethylphosphonium is 140 mV. (5) When delta approximately muH is measured simultaneously on divalent cations and on K+, the values on K+ tend to approach those on Ca2+ while those on Sr2+ are about 50 mV lower. (6) It is concluded that the steady state mitochondrial energy potential is equivalent to a delta approximately muH between 150 and approx. 190 mV. | Proton electrochemical potential in steady state rat liver mitochondria. Delta approximately muH has been determined in steady state mitochondria by measuring the magnitude of delta pH on the distribution of acetate and of deltapsi on the distribution of K+, tetraphenylphosphonium, Ca2+, Sr2+ and Mn2+. (1) The matrix concentration of divalent cations has been calculated from the total cation uptake, from the increase of matrix volume and from the ESR sextet signal of Mn(H2O)L2+. The [cat2+]i based on osmotic data is about five times higher than that based on ESR measurements. The [cat2+]i based on total uptake is much higher than that based on osmotic data at low cation/protein ratios. (2) In the presence of 10 mM acetate the maximal deltapsi on Ca2+ is about 130 mV and on Sr2+ is 95 mV. Deltapsi on Mn2+ is 91 or 109 mV, according to whether [cat2+-a)i is calculated from ESR or osmotic data. Under the same conditions, deltapH is about 60 mV. Hence delta approximately muH on divalent cations is between 151 and 190 mV. (3) Deltapsi on K+, in valinomycin treated mitochondria with 10 mM acetate or 2 mM Pi, drops from 200 mV, at low [K+]0 to almost zero parallel to the increase of [K+]0. DeltapH is 30 mV at low [K+]0 and about 42 mV at 600 muM K+. Hence delta approximately muH drops from 22m mV lower values with the increase of [K+]0. (4) Maximal deltapsi on triphenylmethylphosphonium is 140 mV. (5) When delta approximately muH is measured simultaneously on divalent cations and on K+, the values on K+ tend to approach those on Ca2+ while those on Sr2+ are about 50 mV lower. (6) It is concluded that the steady state mitochondrial energy potential is equivalent to a delta approximately muH between 150 and approx. 190 mV. | [
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PMID:12815 | Role of protein dissociation in the transport of acidic amino acids by the Ehrlich ascites tumor cell. | The pH profile for the uptake of L-glutamic acid by the Ehrlich ascites tumor cell arises largely as a sum of the decline with falling pH of a slow, Na+-dependent uptake by System A, and an increasing uptake by Na+-independent System L. The latter maximizes at about pH 4.5, following approximately the titration curve of the distal carboxyl group. This shift in route of uptake was verified by (a) a declining Na+-dependent component, (b) an almost corresponding decline in the 2-(methylamino)-isobutyric acid-inhibitable component, (c) a rising component inhibited by 2-aminonorbornane-2-carboxylic acid. Other amino acids recognized as principally reactive with Systems A or L yielded corresponding inhibitory effects with some conspicious exceptions: 2-Aminoisobutyric acid and even glycine become better substrates of System L as the pH is lowered; hence their inhibitory action on glutamic acid uptake is not lost. The above results were characterized by generally consistent relations among the half-saturation concentrations of the interacting amino acids with respect to: their own uptake, their inhibition of the uptake, one by another, and their trans stimulation of exodus, one by another. A small Na+-dependent component of uptake retained by L-glutamic acid but not by D-glutamic acid at pH 4.5 is inhibitable by methionine but by neither 2-(methylamino)-isobutyric acid nor the norbornane amino acid. We provisionally identified this component with System ASC, which transports L-glutamine throughout the pH range studied. No transport activity specific to the anionic amino acids was detected, and the unequivocally anionic cysteic acid showed neither significant mediated uptake nor inhibition of the uptake of glutamic aic or of the norbornane amino acid. The dicarboxylic amino acids take the sequence, aspartic acid less than glutamic acid less than alpha-aminoadipic acid less than S-carboxymethylcysteine, in their rate of mediated, Na+-independent uptake at low pH. Diiodotyrosine and two dissimilas isomers of nitrotyrosine also show acceleration of uptake as the phenolate group on the sidechain is protonated, a result indicating that the acidic group need not be a carboxyl group and need not take a specific position in space to be accepted at the receptor site L. The presence of the carboxyl group does not upset the normal stereospecificity of System L until it falls on the beta-carbon in aspartic acid; even then it is the presence of the carbonyl group and not of the intact carboxyl group nor of its hydroxyl group that cancels out the stereospecificity, as was shown by the absence of normal stereospecificity for aspartic acid and asparagine and its presence in glutamic acid, homoserine and glutamine. In agreement, the uptak of aspartic acid is peculiarly sensitive to the presence of an alpha-methyl group or of other structures that modify the orientation of the sidechain. | Role of protein dissociation in the transport of acidic amino acids by the Ehrlich ascites tumor cell. The pH profile for the uptake of L-glutamic acid by the Ehrlich ascites tumor cell arises largely as a sum of the decline with falling pH of a slow, Na+-dependent uptake by System A, and an increasing uptake by Na+-independent System L. The latter maximizes at about pH 4.5, following approximately the titration curve of the distal carboxyl group. This shift in route of uptake was verified by (a) a declining Na+-dependent component, (b) an almost corresponding decline in the 2-(methylamino)-isobutyric acid-inhibitable component, (c) a rising component inhibited by 2-aminonorbornane-2-carboxylic acid. Other amino acids recognized as principally reactive with Systems A or L yielded corresponding inhibitory effects with some conspicious exceptions: 2-Aminoisobutyric acid and even glycine become better substrates of System L as the pH is lowered; hence their inhibitory action on glutamic acid uptake is not lost. The above results were characterized by generally consistent relations among the half-saturation concentrations of the interacting amino acids with respect to: their own uptake, their inhibition of the uptake, one by another, and their trans stimulation of exodus, one by another. A small Na+-dependent component of uptake retained by L-glutamic acid but not by D-glutamic acid at pH 4.5 is inhibitable by methionine but by neither 2-(methylamino)-isobutyric acid nor the norbornane amino acid. We provisionally identified this component with System ASC, which transports L-glutamine throughout the pH range studied. No transport activity specific to the anionic amino acids was detected, and the unequivocally anionic cysteic acid showed neither significant mediated uptake nor inhibition of the uptake of glutamic aic or of the norbornane amino acid. The dicarboxylic amino acids take the sequence, aspartic acid less than glutamic acid less than alpha-aminoadipic acid less than S-carboxymethylcysteine, in their rate of mediated, Na+-independent uptake at low pH. Diiodotyrosine and two dissimilas isomers of nitrotyrosine also show acceleration of uptake as the phenolate group on the sidechain is protonated, a result indicating that the acidic group need not be a carboxyl group and need not take a specific position in space to be accepted at the receptor site L. The presence of the carboxyl group does not upset the normal stereospecificity of System L until it falls on the beta-carbon in aspartic acid; even then it is the presence of the carbonyl group and not of the intact carboxyl group nor of its hydroxyl group that cancels out the stereospecificity, as was shown by the absence of normal stereospecificity for aspartic acid and asparagine and its presence in glutamic acid, homoserine and glutamine. In agreement, the uptak of aspartic acid is peculiarly sensitive to the presence of an alpha-methyl group or of other structures that modify the orientation of the sidechain. | [
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|
PMID:12816 | Proton transport by gastric membrane vesicles. | A highly purified membrane fraction was derived from hog gastric mucosa by a combination of differential and density gradient centrifugation and free flow electrophoresis. This final fraction was 35-fold enriched with respect to cation activated ouabain-insensitive ATPase. Antibody against this fraction was shown to be bound to the luminal surface of the gastric glands. The addition of ATP to this fraction or the density gradient fraction resulted in H+ uptake into an osmotically sensitive space. The apparent Km for ATP was 1.7-10(-4) M in the absence of a K+ gradient similar to that found for ATPase activity. The reaction is specific for ATP and requires cation in the sequence K+ greater than Rb+ greater than Cs+ greater than Na+ greater than Li+ and inhibited by ATPase inhibitors such as N,N'-dicylclohexyl-carbodiimide. Maximal H+ uptake occurs with an outward K+ gradient but the minimal apparent KA is found in the absence of a K+ gradient. The pH optimum for H+ uptake is between 5.8 and 6.2 which corresponds to the pH range for phosphroylation of the enzyme, but is considerably less than the pH maximum of the K+ dependent dephosphorylation. In the presence of an inward K+ gradient, protonophores such as tetrachlorsalicylanilide only partially abolish the H+ gradient but valinomycin dissipates 75% of the gradient, and nigericin abolishes the gradient. The vesicles therefore have a low K+ conductance but a measurable H+ conductance, hence a K+ gradient can produce an H+ gradient in the presence of valinomycin. The uptake and spontaneous leak of H+ are temperature sensitive with a similar transition temperature. Ultraviolet irradiation inactivates ATPase and proton transport at the same rate, approximately at twice the rate of p-nitrophenylphosphatase inactivation. It is concluded that H+ uptake by these vesicles is probably due to a dimeric (H+ + K+)-ATPase and is probably non-electrogenic. | Proton transport by gastric membrane vesicles. A highly purified membrane fraction was derived from hog gastric mucosa by a combination of differential and density gradient centrifugation and free flow electrophoresis. This final fraction was 35-fold enriched with respect to cation activated ouabain-insensitive ATPase. Antibody against this fraction was shown to be bound to the luminal surface of the gastric glands. The addition of ATP to this fraction or the density gradient fraction resulted in H+ uptake into an osmotically sensitive space. The apparent Km for ATP was 1.7-10(-4) M in the absence of a K+ gradient similar to that found for ATPase activity. The reaction is specific for ATP and requires cation in the sequence K+ greater than Rb+ greater than Cs+ greater than Na+ greater than Li+ and inhibited by ATPase inhibitors such as N,N'-dicylclohexyl-carbodiimide. Maximal H+ uptake occurs with an outward K+ gradient but the minimal apparent KA is found in the absence of a K+ gradient. The pH optimum for H+ uptake is between 5.8 and 6.2 which corresponds to the pH range for phosphroylation of the enzyme, but is considerably less than the pH maximum of the K+ dependent dephosphorylation. In the presence of an inward K+ gradient, protonophores such as tetrachlorsalicylanilide only partially abolish the H+ gradient but valinomycin dissipates 75% of the gradient, and nigericin abolishes the gradient. The vesicles therefore have a low K+ conductance but a measurable H+ conductance, hence a K+ gradient can produce an H+ gradient in the presence of valinomycin. The uptake and spontaneous leak of H+ are temperature sensitive with a similar transition temperature. Ultraviolet irradiation inactivates ATPase and proton transport at the same rate, approximately at twice the rate of p-nitrophenylphosphatase inactivation. It is concluded that H+ uptake by these vesicles is probably due to a dimeric (H+ + K+)-ATPase and is probably non-electrogenic. | [
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|
PMID:12817 | Effect of temperature and protonation upon the conformation of 2'-o-methyladenosine. Correlation of conformational parameters in purine nucleosides. | Proton magnetic resonance studies of 2'-o-methyladenosine in 2H2O have been carried out at variable temperature and p2H. The chemical shifts and H-H coupling constants are discussed in terms of the molecular conformation. Comparison of the data with those of adenosine reveals that 2'-O-methylation has little influence on the conformation. At neutral p2H where the adenine base is not protonated, the molecules favor a 2' endo, gauche-gauche conformation. Protonation of the base at the N(1) position leads to a decrease in the 2' endo, gauche-gauche bias. The data for 2'-O-methyladenosine and adenosine, as well as for several other purine derivatives, reveal the presence of a correlation between the sugar pucker and the C(5')-C(4') conformer distribution which is the inverse of the correlation previously reported for pyrimidine derivatives. | Effect of temperature and protonation upon the conformation of 2'-o-methyladenosine. Correlation of conformational parameters in purine nucleosides. Proton magnetic resonance studies of 2'-o-methyladenosine in 2H2O have been carried out at variable temperature and p2H. The chemical shifts and H-H coupling constants are discussed in terms of the molecular conformation. Comparison of the data with those of adenosine reveals that 2'-O-methylation has little influence on the conformation. At neutral p2H where the adenine base is not protonated, the molecules favor a 2' endo, gauche-gauche conformation. Protonation of the base at the N(1) position leads to a decrease in the 2' endo, gauche-gauche bias. The data for 2'-O-methyladenosine and adenosine, as well as for several other purine derivatives, reveal the presence of a correlation between the sugar pucker and the C(5')-C(4') conformer distribution which is the inverse of the correlation previously reported for pyrimidine derivatives. | [
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|
PMID:12818 | [Hydrogen-adduct radicals in thymidine and thymidine 5'-monophosphate photosensitized by proflavin. Protection by sulfur compounds (author's transl)]. | At pH values 5 and 9, the influence of cysteine, cystine, 3-mercaptopropionic acid and S-methylcysteine on the induction of H-adduct radicals in thymidine and thymidine 5'-monophosphate photosensitized by proflavin is investigated. The results obtained indicate that efficient protection is given when the electrostatic interactions between the charged groups of the molecules present allow the close proximity of a thiol or a disulfide bridge and the proflavin - DNAs complex constituent. The scheme proposed for the mechanism involves the capture by the protector of an electron or a proton, indispensable intermediates in the formation of the H-adduct radicals. | [Hydrogen-adduct radicals in thymidine and thymidine 5'-monophosphate photosensitized by proflavin. Protection by sulfur compounds (author's transl)]. At pH values 5 and 9, the influence of cysteine, cystine, 3-mercaptopropionic acid and S-methylcysteine on the induction of H-adduct radicals in thymidine and thymidine 5'-monophosphate photosensitized by proflavin is investigated. The results obtained indicate that efficient protection is given when the electrostatic interactions between the charged groups of the molecules present allow the close proximity of a thiol or a disulfide bridge and the proflavin - DNAs complex constituent. The scheme proposed for the mechanism involves the capture by the protector of an electron or a proton, indispensable intermediates in the formation of the H-adduct radicals. | [
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|
PMID:12819 | Differential, structure-dependent susceptibility of poly(A) and RNA to monomeric and dimeric pancreatic ribonuclease A. | Cross-linked dimers of bovine RNAase A are definitely more efficient than monomers at degrading polyadenylic acid under conditions of ionic strength and pH, where the polymer assumes either a double-helical or an ordered single-stranded, base-stacked structure. The opposite occurs, i.e., monomers of RNAase A are definitely more active than dimers,when poly(A) is digested by the two enzyme species under conditions where the conformation of the polymer is essentially that of a random coil. The same pattern of events occurs when total RNA from Escherichia coli or single-stranded RNA of f2 sus11 bacteriophage are used as substrates under opposite ionic-strength conditions. In the presence of high salt concentrations, favouring the formation and the stability of a secondary structure in self-complementary sequences of RNA, the ribonucleic acids are degraded at a higher rate by dimers than by monomers of bovine RNAase A. The opposite occurs in the presence of very low salt concentrations, i.e. when the RNAs are in solution presumably as random coils. These observations are discussed in the light of a hypothesis already advanced to understand the mechanism of enzymic degradation of secondary structures of polyribonucleotides. | Differential, structure-dependent susceptibility of poly(A) and RNA to monomeric and dimeric pancreatic ribonuclease A. Cross-linked dimers of bovine RNAase A are definitely more efficient than monomers at degrading polyadenylic acid under conditions of ionic strength and pH, where the polymer assumes either a double-helical or an ordered single-stranded, base-stacked structure. The opposite occurs, i.e., monomers of RNAase A are definitely more active than dimers,when poly(A) is digested by the two enzyme species under conditions where the conformation of the polymer is essentially that of a random coil. The same pattern of events occurs when total RNA from Escherichia coli or single-stranded RNA of f2 sus11 bacteriophage are used as substrates under opposite ionic-strength conditions. In the presence of high salt concentrations, favouring the formation and the stability of a secondary structure in self-complementary sequences of RNA, the ribonucleic acids are degraded at a higher rate by dimers than by monomers of bovine RNAase A. The opposite occurs in the presence of very low salt concentrations, i.e. when the RNAs are in solution presumably as random coils. These observations are discussed in the light of a hypothesis already advanced to understand the mechanism of enzymic degradation of secondary structures of polyribonucleotides. | [
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PMID:12820 | Effects of stereochemical structures of tetrahydrobiopterin on tyrosine hydroxylase. | 1. Four stereochemical isomers of tetrahydrobiopterin, i.e., 6-L-erythro-, 6-D-erythro-, 6-L-threo-, or 6-D-threo-1,2-dihydroxypropyltetrahydropterin, have been synthesized and used as cofactors for tyrosine hydroxylase (EC 1.14.18.-) purified from the soluble fraction of bovine adrenal medulla. The L-erythro- (the putative natural cofactor) and D-threo isomers showed a striking similarity in their cofactor activities for tyrosine hydroxylase; the remaining two isomeric tetrahydrobiopterins, D-erythro and L-threo isomers, also had very similar cofactor characteristics. 2. The Km values of the L-erythro and D-threo isomers as cofactor were found to be dependent on their concentrations. When their concentrations were below 100 muM, the Km values of the L-erythro and D-threo isomers were fairly low (about 20 muM). However, the Km values were markedly higher (about 150 muM) at concentrations above 100 muM. The same kinetic behavior was also observed with the tetrahydrobiopterin prepared from a natural source (bullfrog). In contrast, the Km value of the L-threo or D-erythro isomer was found to be independent of the concentration and remained constant throughout the concentration examined. 3. The Km values of tyrosine did not show much difference (from 20 muM to 30 muM) with respect to the structure of the four isomeric cofactors. At high concentrations tyrosine inhibited the enzymatic reaction with any one of the four tetrahydrobiopterin cofactors. 4. Oxygen at high concentrations was also inhibitory with any one of the four stereochemical isomers as cofactor. Approximate Km values for oxygen with the tetrahydrobiopterins as cofactor were 1-5%. 5. In contrast to the four isomers of tetrahydrobiopterin, when 6-methyltetrahydropterin or 6,7-dimethyltetrahydropterin was used as cofactor tyrosine or oxygen did no inhibit the enzymatic reaction at high concentrations, and the Km values toward the pterin cofactor, tyrosine, and oxygen were significantly higher than the Km values with the tetrahydrobiopterins as cofactor. | Effects of stereochemical structures of tetrahydrobiopterin on tyrosine hydroxylase. 1. Four stereochemical isomers of tetrahydrobiopterin, i.e., 6-L-erythro-, 6-D-erythro-, 6-L-threo-, or 6-D-threo-1,2-dihydroxypropyltetrahydropterin, have been synthesized and used as cofactors for tyrosine hydroxylase (EC 1.14.18.-) purified from the soluble fraction of bovine adrenal medulla. The L-erythro- (the putative natural cofactor) and D-threo isomers showed a striking similarity in their cofactor activities for tyrosine hydroxylase; the remaining two isomeric tetrahydrobiopterins, D-erythro and L-threo isomers, also had very similar cofactor characteristics. 2. The Km values of the L-erythro and D-threo isomers as cofactor were found to be dependent on their concentrations. When their concentrations were below 100 muM, the Km values of the L-erythro and D-threo isomers were fairly low (about 20 muM). However, the Km values were markedly higher (about 150 muM) at concentrations above 100 muM. The same kinetic behavior was also observed with the tetrahydrobiopterin prepared from a natural source (bullfrog). In contrast, the Km value of the L-threo or D-erythro isomer was found to be independent of the concentration and remained constant throughout the concentration examined. 3. The Km values of tyrosine did not show much difference (from 20 muM to 30 muM) with respect to the structure of the four isomeric cofactors. At high concentrations tyrosine inhibited the enzymatic reaction with any one of the four tetrahydrobiopterin cofactors. 4. Oxygen at high concentrations was also inhibitory with any one of the four stereochemical isomers as cofactor. Approximate Km values for oxygen with the tetrahydrobiopterins as cofactor were 1-5%. 5. In contrast to the four isomers of tetrahydrobiopterin, when 6-methyltetrahydropterin or 6,7-dimethyltetrahydropterin was used as cofactor tyrosine or oxygen did no inhibit the enzymatic reaction at high concentrations, and the Km values toward the pterin cofactor, tyrosine, and oxygen were significantly higher than the Km values with the tetrahydrobiopterins as cofactor. | [
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PMID:12821 | Partial purification and properties of a cyclic 3',5'-AMP-independent protein kinase from rat liver. | 1. A cyclic 3',5'-AMP-independent protein kinase (ATP : protein phosphotransferase, EC 2.7.1.37) from rat liver cytosol was partially purified and characterized. Purification by (NH4)2SO4 precipitation, DEAE-cellulose, Bio Gel A-0.5 m and cellulose phosphate chromatography increased the specific activity about 700-fold. 2. An endogenous protein substrate was closely associated with the protein kinase and was not separable from this enzyme up to the cellulose phosphate stage. After phosphorylation, chromatography with Bio Gel A-0.5 m partially separated this endogenous phosphoprotein from the enzyme activity; this dissociation had no apparent effect on kinase activity with casein or phosvitin as substrates, or on the apparent molecular weight of the enzyme (approx. 158,000). 3. This protein kinase with casein, phosvitin, or the endogenous substrate was totally insensitive to the thiol reagents, p-hydroxymercuribenzoate, 5,5'-dithiobis(2-nitrobenzoic acid), iodoacetamide, and N-ethylmaleimide. The enzyme was also unaffected by cyclic 3',5'-AMP, heat-stable protein kinase inhibitor, and the regulatory subunit of a cyclic 3',5'-AMP-dependent protein kinase. | Partial purification and properties of a cyclic 3',5'-AMP-independent protein kinase from rat liver. 1. A cyclic 3',5'-AMP-independent protein kinase (ATP : protein phosphotransferase, EC 2.7.1.37) from rat liver cytosol was partially purified and characterized. Purification by (NH4)2SO4 precipitation, DEAE-cellulose, Bio Gel A-0.5 m and cellulose phosphate chromatography increased the specific activity about 700-fold. 2. An endogenous protein substrate was closely associated with the protein kinase and was not separable from this enzyme up to the cellulose phosphate stage. After phosphorylation, chromatography with Bio Gel A-0.5 m partially separated this endogenous phosphoprotein from the enzyme activity; this dissociation had no apparent effect on kinase activity with casein or phosvitin as substrates, or on the apparent molecular weight of the enzyme (approx. 158,000). 3. This protein kinase with casein, phosvitin, or the endogenous substrate was totally insensitive to the thiol reagents, p-hydroxymercuribenzoate, 5,5'-dithiobis(2-nitrobenzoic acid), iodoacetamide, and N-ethylmaleimide. The enzyme was also unaffected by cyclic 3',5'-AMP, heat-stable protein kinase inhibitor, and the regulatory subunit of a cyclic 3',5'-AMP-dependent protein kinase. | [
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PMID:12822 | Stereospecificity of the hydrogen transfer catalyzed by human placental aldose reductase. | Placental aldose reductase (EC 1.1.1.21) was incubated with glucose in the presence of [4A-2H] NADPH prepared in the oxidation of [2-2H] isocitrate by isocitrate dehydrogenase (EC 1.1.1.42) or [4B-2H] NADPH prepared in the oxidation of [1-2H] glucose-6-phosphate dehydrogenase (EC 1.1.1.49). The sorbitol formed from [4A-2H] NADPH contained deuterium and from [4B-2H] NADPH it did not. Therefore, aldose reductase in an A-type enzyme. | Stereospecificity of the hydrogen transfer catalyzed by human placental aldose reductase. Placental aldose reductase (EC 1.1.1.21) was incubated with glucose in the presence of [4A-2H] NADPH prepared in the oxidation of [2-2H] isocitrate by isocitrate dehydrogenase (EC 1.1.1.42) or [4B-2H] NADPH prepared in the oxidation of [1-2H] glucose-6-phosphate dehydrogenase (EC 1.1.1.49). The sorbitol formed from [4A-2H] NADPH contained deuterium and from [4B-2H] NADPH it did not. Therefore, aldose reductase in an A-type enzyme. | [
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|
PMID:12823 | Metal ion-induced conformational changes in Escherichia coli alkaline phosphatase. | Ultraviolet difference spectra are produced by the binding of divalent metal ions to metal-free alkaline phosphatase (EC 3.1.3.1). The interaction of the apoprotein with Zn2+, Mn2+, Co2+ and Cd2+, which induce the tight binding of one phosphate ion per dimer, give distinctly different ultraviolet spectra changes from Ni2+ and Hg2+ which do not induce phosphate binding. Spectrophotometric titrations at alkaline pH of various metallo-enzymes reveal a smaller number of ionizable tyrosines and a greater stability towards alkaline denaturation in the Zn2+- and Mn2+-enzymes than in the Ni2+-, Hg2+- and apoenzymes. The Zn2+- and Mn2+-enzymes have CD spectra in the region of the aromatic transitions that are different from the CD spectra of the Ni2+-, Hg2+- and apoenzymes. Modifications of arginines with 2,3-butanedione show that a smaller number of arginine residues are modified in the Zn2+-enzyme than in the Hg2+-enzyme. The presented data indicate that alkaline phosphatase from Escherichia coli must have a well-defined conformation in order to bind phosphate. Some metal ions (i.e. Zn2+, Co2+, Mn2+ and Cd2+), when interacting with the apoenzyme, alter the conformation of the protein molecule in such a way that it is able to interact with substrate molecules, while other metal ions (i.e. Ni2+ and Hg2+) are incapable of inducing the appropriate conformational change of the apoenzyme. These findings suggest an important structural function of the first two tightly bound metal ions in enzyme. | Metal ion-induced conformational changes in Escherichia coli alkaline phosphatase. Ultraviolet difference spectra are produced by the binding of divalent metal ions to metal-free alkaline phosphatase (EC 3.1.3.1). The interaction of the apoprotein with Zn2+, Mn2+, Co2+ and Cd2+, which induce the tight binding of one phosphate ion per dimer, give distinctly different ultraviolet spectra changes from Ni2+ and Hg2+ which do not induce phosphate binding. Spectrophotometric titrations at alkaline pH of various metallo-enzymes reveal a smaller number of ionizable tyrosines and a greater stability towards alkaline denaturation in the Zn2+- and Mn2+-enzymes than in the Ni2+-, Hg2+- and apoenzymes. The Zn2+- and Mn2+-enzymes have CD spectra in the region of the aromatic transitions that are different from the CD spectra of the Ni2+-, Hg2+- and apoenzymes. Modifications of arginines with 2,3-butanedione show that a smaller number of arginine residues are modified in the Zn2+-enzyme than in the Hg2+-enzyme. The presented data indicate that alkaline phosphatase from Escherichia coli must have a well-defined conformation in order to bind phosphate. Some metal ions (i.e. Zn2+, Co2+, Mn2+ and Cd2+), when interacting with the apoenzyme, alter the conformation of the protein molecule in such a way that it is able to interact with substrate molecules, while other metal ions (i.e. Ni2+ and Hg2+) are incapable of inducing the appropriate conformational change of the apoenzyme. These findings suggest an important structural function of the first two tightly bound metal ions in enzyme. | [
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|
PMID:12824 | Rat intestinal phosphodiesterase II. Properties of the highly purified enzyme and its inactivation by iodoacetic acid. | A highly purifed preparation of rat intestinal phosphodiesterase II (oligonucleate 3'-nucleotidohydrolase, EC 3.1.4.18) has been studied using a synthetic substrate, thymidine 3'(2,4-dinitrophenyl) phosphate. The enzyme was most active between pH 6.1 and pH 6.7 and was inhibited by Cu2+ and Zn2+ but unaffected by EDTA, Mg2+, Co2+, and Ni2+. The reaction rate decreased at high levels of enzyme because of competitive inhibition by deoxythymidine 3'-phosphate, a reaction product, which showed a Ki of 2-10(-5) M. The molecular weight of the enzyme by gel-filtration was 150 000-170 000. In electrofocusing experiments multiple peaks of activity were found at pH 3.4, 4.2-4.5and 7.2. Polyacrylamide gel electrophoresis of freshly purified phosphodiesterase II showed up to 10 protein bands in the gels. If the preparations were stored at 4 degrees C for some time only one or two bands appeared. Investigation of the reaction of rat intestinal phosphodiesterase II with a number of possible phosphodiesterase substrates indicated that the enzyme required a nucleoside 3'-phosphoryl residue for the initiation of hydrolysis. Thus compounds such as NAD, ATP, bis-(p-nitrophenyl)phosphate, thymidine 5'-(p-nitrophenyl)phosphate, glycerylphosphorylcholine, guanylyl-(2' leads to 5')-adenosine and 3',5'-cyclic AMP which contain phosphodiester bonds, nevertheless were not substrates for the enzyme. The enzyme was inhibited reverisbly by p-chloromercuribenzoate and p-chloromercuriphenylsulfonate and inactivated irreversibly by iodoacetic acid. Activity of the phosphodiesterase II was reduced to 50% by incubation with 2.0-10(-3)--5.0-10(-3) M iodoacetate for 20--30 min at 24 degrees C at pH 5.0--6.1. Iodoacetamide had no effect. The degree of inactivation by iodoacetate was reduced by the presence of a substrate for the enzyme or, more effectively by deoxythymidine 3'-phosphate, a competitive inhibitor. It is concluded that iodoacetic acid alkylates an essential residue at the active centre of the enzyme. | Rat intestinal phosphodiesterase II. Properties of the highly purified enzyme and its inactivation by iodoacetic acid. A highly purifed preparation of rat intestinal phosphodiesterase II (oligonucleate 3'-nucleotidohydrolase, EC 3.1.4.18) has been studied using a synthetic substrate, thymidine 3'(2,4-dinitrophenyl) phosphate. The enzyme was most active between pH 6.1 and pH 6.7 and was inhibited by Cu2+ and Zn2+ but unaffected by EDTA, Mg2+, Co2+, and Ni2+. The reaction rate decreased at high levels of enzyme because of competitive inhibition by deoxythymidine 3'-phosphate, a reaction product, which showed a Ki of 2-10(-5) M. The molecular weight of the enzyme by gel-filtration was 150 000-170 000. In electrofocusing experiments multiple peaks of activity were found at pH 3.4, 4.2-4.5and 7.2. Polyacrylamide gel electrophoresis of freshly purified phosphodiesterase II showed up to 10 protein bands in the gels. If the preparations were stored at 4 degrees C for some time only one or two bands appeared. Investigation of the reaction of rat intestinal phosphodiesterase II with a number of possible phosphodiesterase substrates indicated that the enzyme required a nucleoside 3'-phosphoryl residue for the initiation of hydrolysis. Thus compounds such as NAD, ATP, bis-(p-nitrophenyl)phosphate, thymidine 5'-(p-nitrophenyl)phosphate, glycerylphosphorylcholine, guanylyl-(2' leads to 5')-adenosine and 3',5'-cyclic AMP which contain phosphodiester bonds, nevertheless were not substrates for the enzyme. The enzyme was inhibited reverisbly by p-chloromercuribenzoate and p-chloromercuriphenylsulfonate and inactivated irreversibly by iodoacetic acid. Activity of the phosphodiesterase II was reduced to 50% by incubation with 2.0-10(-3)--5.0-10(-3) M iodoacetate for 20--30 min at 24 degrees C at pH 5.0--6.1. Iodoacetamide had no effect. The degree of inactivation by iodoacetate was reduced by the presence of a substrate for the enzyme or, more effectively by deoxythymidine 3'-phosphate, a competitive inhibitor. It is concluded that iodoacetic acid alkylates an essential residue at the active centre of the enzyme. | [
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|
PMID:12825 | Oxidation of methyl derivatives of pteridin-4-one, lumazine and related pteridines by bovine milk xanthine oxidase. | 1. Pteridin-4-ones, methylated at nitrogen or carbon, N-methylated lumazines and related oxopteridines were studied as substrates of a highly purified bovine milk xanthine oxidase (xanthine : oxygen oxidoreductase, EC 1.2.3.2). 2. The enzyme can oxidise at high rates both uncharged and anionic substrates. Variation of enzymic activity with pH is mainly due to pH-dependent changes in the active enzymic center. 3. Milk xanthine oxidases at different stages of purification convert pteridin-4-one into the 4,7-dione (compound 13 in this article). 4. Methylation at C-6 in the pyrazine moiety enhances enzymic attack at C-2 in the pyrimidine ring. N-Methylation may increase or reduce rates of oxidation. 5. For oxidation at C-2, the most favorable form of the substrate bears a double bond at C(2) = N(3). Attack at C-7 is enhanced strongly in structures bearing a double bond at C(6) = C(7). 6. In general, pteridines react with xanthine oxidase as non-hydrated molecules. However, oxidation of 8-methyllumazine at C-7 may take place by dehydrogenation of the 7-CHOH group of the covalently hydrated molecule. | Oxidation of methyl derivatives of pteridin-4-one, lumazine and related pteridines by bovine milk xanthine oxidase. 1. Pteridin-4-ones, methylated at nitrogen or carbon, N-methylated lumazines and related oxopteridines were studied as substrates of a highly purified bovine milk xanthine oxidase (xanthine : oxygen oxidoreductase, EC 1.2.3.2). 2. The enzyme can oxidise at high rates both uncharged and anionic substrates. Variation of enzymic activity with pH is mainly due to pH-dependent changes in the active enzymic center. 3. Milk xanthine oxidases at different stages of purification convert pteridin-4-one into the 4,7-dione (compound 13 in this article). 4. Methylation at C-6 in the pyrazine moiety enhances enzymic attack at C-2 in the pyrimidine ring. N-Methylation may increase or reduce rates of oxidation. 5. For oxidation at C-2, the most favorable form of the substrate bears a double bond at C(2) = N(3). Attack at C-7 is enhanced strongly in structures bearing a double bond at C(6) = C(7). 6. In general, pteridines react with xanthine oxidase as non-hydrated molecules. However, oxidation of 8-methyllumazine at C-7 may take place by dehydrogenation of the 7-CHOH group of the covalently hydrated molecule. | [
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|
PMID:12826 | Purification and properties of rabbit heart muscle aldolase. | Fructose diphosphate aldolase (D-fructose-1,6-biphosphate D-glyceraldehyde-3-phosphate lyase, EC 4.1.2.13) from rabbit heart has been purified and obtained in crystalline form. The preparations are homogeneous on the basis of disc gel electrophoresis and ultracentrifugation. The catalytic and the molecular properties indicate that this is aldolase A. A comparison was made between rabbit heart aldolase and the rabbit muscle enzyme. The sedimentation coefficient, energy of activation and Michaelis constant for Fru-1,6-P2 were found to be identical with the values obtained for the muscle enzyme. As in case of the muscle enzyme, heart aldolase was found to have a broad pH optimum, remarkable stability over a wide pH range, and the ability to form a Schiff base intermediate with dihydroxyacetone phosphate upon reduction with borohydride. Cleavage of the methionyl bonds with CNBr yields the same pattern as obtained with the muscle enzyme. | Purification and properties of rabbit heart muscle aldolase. Fructose diphosphate aldolase (D-fructose-1,6-biphosphate D-glyceraldehyde-3-phosphate lyase, EC 4.1.2.13) from rabbit heart has been purified and obtained in crystalline form. The preparations are homogeneous on the basis of disc gel electrophoresis and ultracentrifugation. The catalytic and the molecular properties indicate that this is aldolase A. A comparison was made between rabbit heart aldolase and the rabbit muscle enzyme. The sedimentation coefficient, energy of activation and Michaelis constant for Fru-1,6-P2 were found to be identical with the values obtained for the muscle enzyme. As in case of the muscle enzyme, heart aldolase was found to have a broad pH optimum, remarkable stability over a wide pH range, and the ability to form a Schiff base intermediate with dihydroxyacetone phosphate upon reduction with borohydride. Cleavage of the methionyl bonds with CNBr yields the same pattern as obtained with the muscle enzyme. | [
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|
PMID:12827 | A cis-trans isomerising activity of Escherichia coli. Isomerization from 2-(2-furyl)-3-cis-(5-nitro-2-furyl) acrylamide (furylfuramide) to its trans isomer. | The soluble enzyme fraction derived from Escherichia coli K-12 JE2100 cells was found to exhibit, in addition to Nadh- and NADPH-dependent reductase activities, NADH-dependent cis-trans isomerising activity toward 2-(2-furyl-3-(5-nitro-2-furyl)acrylamide leading to a specific change in geometrical configuration of the vinyl group at the 2-position from cis to trans but not in the reverse direction. This furylfuramide-isomerising action of bacteria was dicoumarol insensitive, and did not require glutathione for full activity. The particulate enzyme fraction derived from JE2100 cells, although it showed little reductase activity toward furylfuramide in the presence of either NADH or NADPH, revealed an isomerising activity in the presence of NADH. | A cis-trans isomerising activity of Escherichia coli. Isomerization from 2-(2-furyl)-3-cis-(5-nitro-2-furyl) acrylamide (furylfuramide) to its trans isomer. The soluble enzyme fraction derived from Escherichia coli K-12 JE2100 cells was found to exhibit, in addition to Nadh- and NADPH-dependent reductase activities, NADH-dependent cis-trans isomerising activity toward 2-(2-furyl-3-(5-nitro-2-furyl)acrylamide leading to a specific change in geometrical configuration of the vinyl group at the 2-position from cis to trans but not in the reverse direction. This furylfuramide-isomerising action of bacteria was dicoumarol insensitive, and did not require glutathione for full activity. The particulate enzyme fraction derived from JE2100 cells, although it showed little reductase activity toward furylfuramide in the presence of either NADH or NADPH, revealed an isomerising activity in the presence of NADH. | [
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|
PMID:12828 | Influence of 8-substitutes on the oxidation of hypoxanthine and 6-thioxopurine by bovine milk xanthine oxidase. | 1. The influence of 8-substituents was studied on the rate of oxidation of hypoxanthine and 6-thioxopurine by bovine milk xanthine oxidase (EC 1.2.3.2). 2. An 8-methyl group does not alter the rate of oxidation of hypoxanthine materially, but an 8-phenyl substituent reduces it markedly. This is ascribed to inhibition of the tautomerisation process, responsible for substrate activation, prior to oxidation. 3. In contrast, the 8-phenyl group in 3-methyl-8-phenylhypoxanthine enhances the rate, presumably by binding to a hydrophobic site near the enzymaic center. 4. An 8-phenyl group in 6-thioxopurine markedly increases the rate of enzymaic oxidation. Probably the aromatic substituent diverts anion formation to the imidazole ring. In contrast, ionisation of 8-methyl-6-thioxopurine involves the pyrimidine moiety, thus rendering enzymic attack at position 2 more difficult. | Influence of 8-substitutes on the oxidation of hypoxanthine and 6-thioxopurine by bovine milk xanthine oxidase. 1. The influence of 8-substituents was studied on the rate of oxidation of hypoxanthine and 6-thioxopurine by bovine milk xanthine oxidase (EC 1.2.3.2). 2. An 8-methyl group does not alter the rate of oxidation of hypoxanthine materially, but an 8-phenyl substituent reduces it markedly. This is ascribed to inhibition of the tautomerisation process, responsible for substrate activation, prior to oxidation. 3. In contrast, the 8-phenyl group in 3-methyl-8-phenylhypoxanthine enhances the rate, presumably by binding to a hydrophobic site near the enzymaic center. 4. An 8-phenyl group in 6-thioxopurine markedly increases the rate of enzymaic oxidation. Probably the aromatic substituent diverts anion formation to the imidazole ring. In contrast, ionisation of 8-methyl-6-thioxopurine involves the pyrimidine moiety, thus rendering enzymic attack at position 2 more difficult. | [
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|
PMID:12829 | Transhydrogenase activity in the marine bacterium Beneckea natriegens. | The marine bacterium, Beneckea natriegens, which has previously been reported not to form transhydrogenase, has been shown to synthesize a soluble energy-independent transhydrogenase (NADPH:NADP+ oxidoreductase, EC 1.6.1.1), though no energy-linked activity could be detected. The transhydrogenase is induced maximally in stationary phase cells and its formation is 70-90% repressed by raising the medium phosphate level from 0.33 to 3.3 mM. The enzyme is inhibited by arsenate, inorganic ortho- and pyrophosphate and by a range of organic phosphate-containing compounds, including 2'-AMP, which is an activator of several bacterial transhydrogenases. | Transhydrogenase activity in the marine bacterium Beneckea natriegens. The marine bacterium, Beneckea natriegens, which has previously been reported not to form transhydrogenase, has been shown to synthesize a soluble energy-independent transhydrogenase (NADPH:NADP+ oxidoreductase, EC 1.6.1.1), though no energy-linked activity could be detected. The transhydrogenase is induced maximally in stationary phase cells and its formation is 70-90% repressed by raising the medium phosphate level from 0.33 to 3.3 mM. The enzyme is inhibited by arsenate, inorganic ortho- and pyrophosphate and by a range of organic phosphate-containing compounds, including 2'-AMP, which is an activator of several bacterial transhydrogenases. | [
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|
PMID:12830 | Reactions of the Neurospora crassa nitrate reductase with NAD(P) analogs. | The assimilatory NADPH-nitrate reductase (NADPH:nitrate oxidoreductase, EC 1.6.6.3) from Neurospora crassa is competitively inhibited by 3-aminopyridine adenine dinucleotide (AAD) and 3-aminopyridine adenine dinucleotide phosphate (AADP) which are structural analogs of NAD and NADP, respectively. The amino group of the pyridine ring of AAD(P) can react with nitrous acid to yield the diazonium derivative which may covalently bind at the NAD(P) site. As a result of covalent attachment, diazotized AAD(P) causes time-dependent irreversible inactivation of nitrate reductase. However, only the NADPH-dependent activities of the nitrate reductase, i.e. the overall NADPH-nitrate reductase and the NADPH-cytochrome c reductase activities, are inactivated. The reduced methyl viologen- and reduced FAD-nitrate reductase activities which do not utilize NADPH are not inhibited. This inactivation by diazotized AADP is prevented by 1 mM NADP. The inclusion of 1 muM FAD can also prevent inactivation, but the FAD effect differs from the NADP protection in that even after removal of the exogenous FAD by extensive dialysis or Sephadex G-25 filtration chromatography, the enzyme is still protected against inactivation. The FAD-generated protected form of nitrate reductase could again be inactivated if the enzyme was treated with NADPH, dialyzed to remove the NADPH, and then exposed to diazotized AADP. When NADP was substituted for NADPH in this experiment, the enzyme remained in the FAD-protected state. Difference spectra of the inactivated nitrate reductase demonstrated the presence of bound AADP, and titration of the sulfhydryl groups of the inactivated enzyme revealed that a loss of accessible sulfhydryls had occurred. The hypothesis generated by these experiments is that diazotized AADP binds at the NADPH site on nitrate reductase and reacts with a functional sulfhydryl at the site. FAD protects the enzyme against inactivation by modifying the sulfhydryl. Since NADPH reverses this protection, it appears the modifications occurring are oxidation-reduction reactions. On the basis of these results, the physiological electron flow in the nitrate reductase is postulated to be from NADPH via sulfhydryls to FAD and then the remainder of the electron carriers as follows: NADPH leads to -SH leads to FAD leads to cytochrome b-557 leads to Mo leads to NO-3. | Reactions of the Neurospora crassa nitrate reductase with NAD(P) analogs. The assimilatory NADPH-nitrate reductase (NADPH:nitrate oxidoreductase, EC 1.6.6.3) from Neurospora crassa is competitively inhibited by 3-aminopyridine adenine dinucleotide (AAD) and 3-aminopyridine adenine dinucleotide phosphate (AADP) which are structural analogs of NAD and NADP, respectively. The amino group of the pyridine ring of AAD(P) can react with nitrous acid to yield the diazonium derivative which may covalently bind at the NAD(P) site. As a result of covalent attachment, diazotized AAD(P) causes time-dependent irreversible inactivation of nitrate reductase. However, only the NADPH-dependent activities of the nitrate reductase, i.e. the overall NADPH-nitrate reductase and the NADPH-cytochrome c reductase activities, are inactivated. The reduced methyl viologen- and reduced FAD-nitrate reductase activities which do not utilize NADPH are not inhibited. This inactivation by diazotized AADP is prevented by 1 mM NADP. The inclusion of 1 muM FAD can also prevent inactivation, but the FAD effect differs from the NADP protection in that even after removal of the exogenous FAD by extensive dialysis or Sephadex G-25 filtration chromatography, the enzyme is still protected against inactivation. The FAD-generated protected form of nitrate reductase could again be inactivated if the enzyme was treated with NADPH, dialyzed to remove the NADPH, and then exposed to diazotized AADP. When NADP was substituted for NADPH in this experiment, the enzyme remained in the FAD-protected state. Difference spectra of the inactivated nitrate reductase demonstrated the presence of bound AADP, and titration of the sulfhydryl groups of the inactivated enzyme revealed that a loss of accessible sulfhydryls had occurred. The hypothesis generated by these experiments is that diazotized AADP binds at the NADPH site on nitrate reductase and reacts with a functional sulfhydryl at the site. FAD protects the enzyme against inactivation by modifying the sulfhydryl. Since NADPH reverses this protection, it appears the modifications occurring are oxidation-reduction reactions. On the basis of these results, the physiological electron flow in the nitrate reductase is postulated to be from NADPH via sulfhydryls to FAD and then the remainder of the electron carriers as follows: NADPH leads to -SH leads to FAD leads to cytochrome b-557 leads to Mo leads to NO-3. | [
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|
PMID:12831 | Purification and characterization of cholesterol esterase from porcine pancreas. | A protein catalyzing the hydrolysis of cholesterol esters and p-nitrophenyl acetate has been purified 200-fold from porcine pancreas. The enzyme is homogenous as judged by polyacrylamide gel electrophoresis and exhibits a molecular weight of 80 000 as determined by sodium dodecyl sulfate electrophoresis and gel filtration. Activity toward p-nitrophenylacetate exhibits a broad pH optimum and is influenced by a group with a pKa of 5.5--6.0. The enzyme is completely inhibited by diisopropylfluorophosphate at concentrations as low as 10(-5) M, suggesting that it is a serine esterase. Partial inhibition was observed with p-chloromercuribenzoate. | Purification and characterization of cholesterol esterase from porcine pancreas. A protein catalyzing the hydrolysis of cholesterol esters and p-nitrophenyl acetate has been purified 200-fold from porcine pancreas. The enzyme is homogenous as judged by polyacrylamide gel electrophoresis and exhibits a molecular weight of 80 000 as determined by sodium dodecyl sulfate electrophoresis and gel filtration. Activity toward p-nitrophenylacetate exhibits a broad pH optimum and is influenced by a group with a pKa of 5.5--6.0. The enzyme is completely inhibited by diisopropylfluorophosphate at concentrations as low as 10(-5) M, suggesting that it is a serine esterase. Partial inhibition was observed with p-chloromercuribenzoate. | [
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|
PMID:12832 | Conversion of 9-D- and 13-L-hydroperoxylinoleic acids by soybean lipoxygenase-1 under anaerobic conditions. | Soybean lipoxygenase-1 reacts with both 9-D and 13-L-hydroperoxylinoleic acids under anaerobic conditions. Approximately 40% of the hydroperoxide is converted into oxodienes, absorbing at 285 nm. Concomitantly, more polar compounds are formed, tentatively identified as being mainly epoxy-hydroxy-octadecenoic acids. When oxygen is present, the reaction is strongly inhibited, until in a very slow reaction the oxygen has been depleted. This accounts for the occurrence of a lag period. | Conversion of 9-D- and 13-L-hydroperoxylinoleic acids by soybean lipoxygenase-1 under anaerobic conditions. Soybean lipoxygenase-1 reacts with both 9-D and 13-L-hydroperoxylinoleic acids under anaerobic conditions. Approximately 40% of the hydroperoxide is converted into oxodienes, absorbing at 285 nm. Concomitantly, more polar compounds are formed, tentatively identified as being mainly epoxy-hydroxy-octadecenoic acids. When oxygen is present, the reaction is strongly inhibited, until in a very slow reaction the oxygen has been depleted. This accounts for the occurrence of a lag period. | [
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PMID:12833 | Kinetic study of lipoxygenase-hydroperoxylinoleic acid interaction. | Interaction of lipoxygenase with hydroperoxylinoleic acid, which is the product of this enzyme reaction and acts as an activator, was studied kinetically by the fluorescence stopped-flow method. The kinetic features are consistent with a two-step mechanism involving a fast bimolecular association process followed by a slow unimolecular process. The dissociation constant of the bimolecular process was 3 (+/-2) - 10(-5) M, which was appreciably dependent on temperature and pH, in contrast to the rate constant of the latter process. The enthalpy and the entropy of activation for the unimolecular process were estimated to be 21 kcal/mol and 20 e.u., respectively. The pH dependence of the rate constant indicated that an ionizable group with pK of about 8.6 is involved in the interaction. Linoleic acid, the substrate of lipoxygenase, and oleic acid inhibited the interaction between the lipoxygenase and the hydroperoxylinoleic acid by reducing the rate. A series of saturated monohydric alcohols also reduced the rate of the interaction as the chain length of the alcohols increases, though methanol and ethanol increased the rate of the interaction. | Kinetic study of lipoxygenase-hydroperoxylinoleic acid interaction. Interaction of lipoxygenase with hydroperoxylinoleic acid, which is the product of this enzyme reaction and acts as an activator, was studied kinetically by the fluorescence stopped-flow method. The kinetic features are consistent with a two-step mechanism involving a fast bimolecular association process followed by a slow unimolecular process. The dissociation constant of the bimolecular process was 3 (+/-2) - 10(-5) M, which was appreciably dependent on temperature and pH, in contrast to the rate constant of the latter process. The enthalpy and the entropy of activation for the unimolecular process were estimated to be 21 kcal/mol and 20 e.u., respectively. The pH dependence of the rate constant indicated that an ionizable group with pK of about 8.6 is involved in the interaction. Linoleic acid, the substrate of lipoxygenase, and oleic acid inhibited the interaction between the lipoxygenase and the hydroperoxylinoleic acid by reducing the rate. A series of saturated monohydric alcohols also reduced the rate of the interaction as the chain length of the alcohols increases, though methanol and ethanol increased the rate of the interaction. | [
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|
PMID:12834 | Studies on the metabolism of beta-carotene and apo-beta-carotenoids in rats and chickens. | (1)The relative abilities of the various fractions of rat and chicken liver to oxidize and reduce retinal and 8'-and 12'-apo-beta-carotenal were investigatjed and it has been shown that, while retinal is exclusely oxidized by the soluble fraction, the apocarotenals are mostly oxidized by the particulate fractions of the homogenate. (2) Addition of NAD+ or NADP+ markedly activated the oxidation of the apocarotenals, but not of retinal by the particulate fractions. (3) Considerable amounts of retinal and 8'-, 10'- and 12'-apo-beta-carotenal were isolated from the intestine of chickens fed beta-carotene and these apocarotenoids were conclusively identified. (4) Significant amounts of 8'-, 10'- and 12'-apo-beta-carotenoic acids were isolated from the intestine of rats given 8'-apo-beta-carotenal and these apocarotenoic acids were also conclusively identified. (5) In the light of these observations it is suggested that during conversion to vitamin A, the beta-carotene molecule is simultaneously attacked by the dioxygenase at several double bonds, the primary attack being at the central double bond and a tentative scheme for the mechanism of conversion is proposed. | Studies on the metabolism of beta-carotene and apo-beta-carotenoids in rats and chickens. (1)The relative abilities of the various fractions of rat and chicken liver to oxidize and reduce retinal and 8'-and 12'-apo-beta-carotenal were investigatjed and it has been shown that, while retinal is exclusely oxidized by the soluble fraction, the apocarotenals are mostly oxidized by the particulate fractions of the homogenate. (2) Addition of NAD+ or NADP+ markedly activated the oxidation of the apocarotenals, but not of retinal by the particulate fractions. (3) Considerable amounts of retinal and 8'-, 10'- and 12'-apo-beta-carotenal were isolated from the intestine of chickens fed beta-carotene and these apocarotenoids were conclusively identified. (4) Significant amounts of 8'-, 10'- and 12'-apo-beta-carotenoic acids were isolated from the intestine of rats given 8'-apo-beta-carotenal and these apocarotenoic acids were also conclusively identified. (5) In the light of these observations it is suggested that during conversion to vitamin A, the beta-carotene molecule is simultaneously attacked by the dioxygenase at several double bonds, the primary attack being at the central double bond and a tentative scheme for the mechanism of conversion is proposed. | [
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|
PMID:12835 | Very low density lipoprotein. Dissociation of apolipoprotein C during lipoprotein lipase induced lipolysis. | The fate of apo C in rat plasma very low density lipoprotein (VLDL) during lipolysis was studied using VLDL labeled specifically with 125I-labeled apo C and purified bovine milk lipoprotein lipase. Incubations were carried out in vitro and included serum-containing systems and albumin containing systems. Free fatty acids generation proceeded with time of incubation in the two systems. It, however, was enhanced 1.5--2 fold by the presence of serum. 125I-labeled apo C equilibrated between very low and high density lipoprotein (HDL) in both systems even when enzyme was not present in the incubation medium, or when the incubation was carried out at 0 degrees C. Upon initiation of lipolysis, more 125I-labeled apo C was transferred to HDL and the transfer was proportional to the magnitude of free fatty acids release. 125I-labeled apo C was also progressively removed from VLDL in the albumin-containing system, although no known lipoprotein acceptor to apo C was present in the medium. The 125I-labeled apo C was recovered predominantly with the medium fraction of d greater than 1.21 g/ml (60--70%), and to a lesser degree with that of d= 1.019--1.21 g/ml. However, the relationship between lipolysis (measured as free fatty acids release) and removal of 125I-labeled apo C from VLDL were indistinguinshable in the albumin containing system and the serum containing system. On the basis of these observations, it is postulated that the removal of apo C during lipolysis of VLDL reflects the nature of the partially degraded VLDL particles, and is independent of the presence of a lipoprotein acceptor to apo C. | Very low density lipoprotein. Dissociation of apolipoprotein C during lipoprotein lipase induced lipolysis. The fate of apo C in rat plasma very low density lipoprotein (VLDL) during lipolysis was studied using VLDL labeled specifically with 125I-labeled apo C and purified bovine milk lipoprotein lipase. Incubations were carried out in vitro and included serum-containing systems and albumin containing systems. Free fatty acids generation proceeded with time of incubation in the two systems. It, however, was enhanced 1.5--2 fold by the presence of serum. 125I-labeled apo C equilibrated between very low and high density lipoprotein (HDL) in both systems even when enzyme was not present in the incubation medium, or when the incubation was carried out at 0 degrees C. Upon initiation of lipolysis, more 125I-labeled apo C was transferred to HDL and the transfer was proportional to the magnitude of free fatty acids release. 125I-labeled apo C was also progressively removed from VLDL in the albumin-containing system, although no known lipoprotein acceptor to apo C was present in the medium. The 125I-labeled apo C was recovered predominantly with the medium fraction of d greater than 1.21 g/ml (60--70%), and to a lesser degree with that of d= 1.019--1.21 g/ml. However, the relationship between lipolysis (measured as free fatty acids release) and removal of 125I-labeled apo C from VLDL were indistinguinshable in the albumin containing system and the serum containing system. On the basis of these observations, it is postulated that the removal of apo C during lipolysis of VLDL reflects the nature of the partially degraded VLDL particles, and is independent of the presence of a lipoprotein acceptor to apo C. | [
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|
PMID:12836 | Studies on the biosynthesis of acylphosphatidylglycerol in Escherichia coli B and B/r. | The present study has demonstrated that one molecule of acylphosphatidylglycerol was synthesized from two molecules of phosphatidylgycerol by the transacylation reaction in which phosphatidylglycerol acted both as an acyl donor and an acceptor. Phosphatidylethanolamine was identified as an another acyl donor, participating in acylphosphatidylglycerol formation. These results are discussed in terms of a new pathway for the turnover of phosphatidylglycerol in Escherichia coli. | Studies on the biosynthesis of acylphosphatidylglycerol in Escherichia coli B and B/r. The present study has demonstrated that one molecule of acylphosphatidylglycerol was synthesized from two molecules of phosphatidylgycerol by the transacylation reaction in which phosphatidylglycerol acted both as an acyl donor and an acceptor. Phosphatidylethanolamine was identified as an another acyl donor, participating in acylphosphatidylglycerol formation. These results are discussed in terms of a new pathway for the turnover of phosphatidylglycerol in Escherichia coli. | [
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|
PMID:12837 | Inhibition of in vitro cholesterol synthesis by fatty acids. | Inhibitory effect of 44 species of fatty acids on cholesterol synthesis has been examined with a rat liver enzyme system. In the case of saturated fatty acids, the inhibitory activity increased with chain length to a maximum at 11 to 14 carbons, after which activity decreased rapidly. The inhibition increased with the degree of unsaturation of fatty acids. Introduction of a hydroxy group at the alpha-position of fatty acids abolished the inhibition, while the inhibition was enhanced by the presence of a hydroxy group located in an intermediate position of the chain. Branched chain fatty acids having a methyl group at the terminal showed much higher activity than the corresponding saturated straight chain fatty acids with the same number of carbons. With respect to the mechanism for inhibition, tridecanoate was found to inhibit acetoacetyl-CoA thiolase specifically without affecting the other reaction steps in the cholesterol synthetic pathway. The highly unsaturated fatty acids, arachidonate and linoleate, were specific inhibitors of 3-hydroxy-3-methyl-glutaryl-CoA synthase. On the other hand, ricinoleate (hydroxy acid) and phytanate (branched-chain acid) diminished the conversion of mevalonate to sterols by inhibiting a step or steps between squalene and lanosterol. | Inhibition of in vitro cholesterol synthesis by fatty acids. Inhibitory effect of 44 species of fatty acids on cholesterol synthesis has been examined with a rat liver enzyme system. In the case of saturated fatty acids, the inhibitory activity increased with chain length to a maximum at 11 to 14 carbons, after which activity decreased rapidly. The inhibition increased with the degree of unsaturation of fatty acids. Introduction of a hydroxy group at the alpha-position of fatty acids abolished the inhibition, while the inhibition was enhanced by the presence of a hydroxy group located in an intermediate position of the chain. Branched chain fatty acids having a methyl group at the terminal showed much higher activity than the corresponding saturated straight chain fatty acids with the same number of carbons. With respect to the mechanism for inhibition, tridecanoate was found to inhibit acetoacetyl-CoA thiolase specifically without affecting the other reaction steps in the cholesterol synthetic pathway. The highly unsaturated fatty acids, arachidonate and linoleate, were specific inhibitors of 3-hydroxy-3-methyl-glutaryl-CoA synthase. On the other hand, ricinoleate (hydroxy acid) and phytanate (branched-chain acid) diminished the conversion of mevalonate to sterols by inhibiting a step or steps between squalene and lanosterol. | [
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|
PMID:12839 | Purification and properties of acid phosphatases isolated from Owenia fusiformis. | Acid phosphatase (EC. 3.1.3.2) has been separated by molecular sieving into two fractions and these fractions were purified by Sephadex ion-exchange chromatography. One of the purified enzymes (fraction II) was purified 830 fold and had a specific activity of 34 international units per mg protein at 37 degrees C and at a pH of 4.9. The Km value with p-nitrophenylphosphate as substrate was 9.10(-4) M and the kinetic studies showed no possibilities of control by allosteric transitions, and no effect of metabolites (amino acids) on the reaction velocity. | Purification and properties of acid phosphatases isolated from Owenia fusiformis. Acid phosphatase (EC. 3.1.3.2) has been separated by molecular sieving into two fractions and these fractions were purified by Sephadex ion-exchange chromatography. One of the purified enzymes (fraction II) was purified 830 fold and had a specific activity of 34 international units per mg protein at 37 degrees C and at a pH of 4.9. The Km value with p-nitrophenylphosphate as substrate was 9.10(-4) M and the kinetic studies showed no possibilities of control by allosteric transitions, and no effect of metabolites (amino acids) on the reaction velocity. | [
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|
PMID:12838 | [Biphasic nature of the light-dependent transport of C14-alanine into Halobacterium holobium cells]. | Biphase character of photoinduced pH change in H. halobium R1 suspension cells is shown: in the first illumination period pH rises and only afterwards it decreases. pH increase is accompanied by the introduction of C14-alanine into the cells, while the decrease by its yield up to the level lower than the "dark" one ("negative" photoeffect). The bi-phase character of transport processes seems to be explained by the reversible character of light-dependent bacteriorodopsin proton pump in H. halobium R1 cells. | [Biphasic nature of the light-dependent transport of C14-alanine into Halobacterium holobium cells]. Biphase character of photoinduced pH change in H. halobium R1 suspension cells is shown: in the first illumination period pH rises and only afterwards it decreases. pH increase is accompanied by the introduction of C14-alanine into the cells, while the decrease by its yield up to the level lower than the "dark" one ("negative" photoeffect). The bi-phase character of transport processes seems to be explained by the reversible character of light-dependent bacteriorodopsin proton pump in H. halobium R1 cells. | [
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|
PMID:12845 | Prothrombin complex concentrates: potentially thrombogenic materials and clues to the mechanism of thrombosis in vivo. | Factors affecting the coagulant activity of two different prothrombin complex concentrates have been investigated using a sensitive in vitro assay developed in this laboratory. One concentrate contained substantial amounts of potentially thrombogenic material, while the other, which was deliberately fortified with antithrombin III and heparin during production, was judged to be relatively nonthrombogenic. The coagulant activity of the thrombogenic concentrate has been partially identified and was due largely to the presence of coagulation factos IXa and Xa. Neither concentrate contained detectable thrombin. However, after incubation with calcium or various polyamines, large amounts of additional coagulant material, including thrombin, appeared. Heparin and antithrombin III not only neutralized the thrombogenic materials present in the thrombogenic concentrate, but also inhibited the de novo generation of coagulant enzymes during incubation with calcium. The implication of these studies on the preparation of prothrombin complex concentrates and on host susceptibility to thrombosis during the clinical use of these concentrates is discussed. | Prothrombin complex concentrates: potentially thrombogenic materials and clues to the mechanism of thrombosis in vivo. Factors affecting the coagulant activity of two different prothrombin complex concentrates have been investigated using a sensitive in vitro assay developed in this laboratory. One concentrate contained substantial amounts of potentially thrombogenic material, while the other, which was deliberately fortified with antithrombin III and heparin during production, was judged to be relatively nonthrombogenic. The coagulant activity of the thrombogenic concentrate has been partially identified and was due largely to the presence of coagulation factos IXa and Xa. Neither concentrate contained detectable thrombin. However, after incubation with calcium or various polyamines, large amounts of additional coagulant material, including thrombin, appeared. Heparin and antithrombin III not only neutralized the thrombogenic materials present in the thrombogenic concentrate, but also inhibited the de novo generation of coagulant enzymes during incubation with calcium. The implication of these studies on the preparation of prothrombin complex concentrates and on host susceptibility to thrombosis during the clinical use of these concentrates is discussed. | [
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|
PMID:12846 | G-6-PD Long Prairie: a new glucose-6-phosphate dehydrogenase mutant exhibiting normal sensitivity to inhibition by NADPH and accompanied by nonspherocytic hemolytic anemia. | The enzymatic properties of a new glucose-6-phosphate dehydrogenase (G-6-PD) variant (G-6-PD Long Prairie) were studied in a white patient with chronic nonspherocytic hemolysis. The red cells were found to have 2.3%-7.7% normal enzymatic activity. The mutant enzyme exhibited marked heat instability, an increased pH optimum, a moderately decreased Km for G-6-P, and increased utilization of 2-deoxyglucose-6-phosphate and deamino NADP. The Km for NADP and Ki for NADPH were both normal. G-6-PD Long Prairie is an interesting new G-6-PD variant that demonstrates that chronic hemolysis can be associated with modestly decreased G-6-PD activity despite normal sensitivity to inhibition by NADPH. Although increased sensitivity to inhibition by NADPH has been postulated to decrease intracellular enzyme activity, resulting in enhanced susceptibility to hemolysis in certain G-6-PD variants with only moderately decreased enzymatic activity, an alternative mechanism of hemolysis, possibly enzyme thermolability, exists in G-6-PD Long Prairie. | G-6-PD Long Prairie: a new glucose-6-phosphate dehydrogenase mutant exhibiting normal sensitivity to inhibition by NADPH and accompanied by nonspherocytic hemolytic anemia. The enzymatic properties of a new glucose-6-phosphate dehydrogenase (G-6-PD) variant (G-6-PD Long Prairie) were studied in a white patient with chronic nonspherocytic hemolysis. The red cells were found to have 2.3%-7.7% normal enzymatic activity. The mutant enzyme exhibited marked heat instability, an increased pH optimum, a moderately decreased Km for G-6-P, and increased utilization of 2-deoxyglucose-6-phosphate and deamino NADP. The Km for NADP and Ki for NADPH were both normal. G-6-PD Long Prairie is an interesting new G-6-PD variant that demonstrates that chronic hemolysis can be associated with modestly decreased G-6-PD activity despite normal sensitivity to inhibition by NADPH. Although increased sensitivity to inhibition by NADPH has been postulated to decrease intracellular enzyme activity, resulting in enhanced susceptibility to hemolysis in certain G-6-PD variants with only moderately decreased enzymatic activity, an alternative mechanism of hemolysis, possibly enzyme thermolability, exists in G-6-PD Long Prairie. | [
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|
PMID:12847 | Experience with incompatible maternal donors for bone marrow transplantation. | Marrow transplantation in aplastic anemia and leukemia has generally been limited to siblings who have been histocompatible at both the serological (A and B) and lymphocyte determined (D or MLC) loci of the HLA system. We studied three male patients, two with aplastic anemia and one with acute myelogenous leukemia, who received transplants from their histoincompatible mothers. MLC studies between donors and recipients showed varying degrees of stimulation. Definite engraftment occurred in one patient and transient engraftment in another. Engraftment in the third patient could not be evaluated. In the patient with sustained engraftment, there was clinical evidence of severe graft versus host disease (GVHD) however, this was not substantiated by histologic findings. This preliminary study suggests that MLC incompatibility may be more of an indicator of the risk of GVHD than of bone marrow rejection. If more effective control of GVHD can be accomplished, marrow transplantation between MLC-reactive individuals may become feasible. | Experience with incompatible maternal donors for bone marrow transplantation. Marrow transplantation in aplastic anemia and leukemia has generally been limited to siblings who have been histocompatible at both the serological (A and B) and lymphocyte determined (D or MLC) loci of the HLA system. We studied three male patients, two with aplastic anemia and one with acute myelogenous leukemia, who received transplants from their histoincompatible mothers. MLC studies between donors and recipients showed varying degrees of stimulation. Definite engraftment occurred in one patient and transient engraftment in another. Engraftment in the third patient could not be evaluated. In the patient with sustained engraftment, there was clinical evidence of severe graft versus host disease (GVHD) however, this was not substantiated by histologic findings. This preliminary study suggests that MLC incompatibility may be more of an indicator of the risk of GVHD than of bone marrow rejection. If more effective control of GVHD can be accomplished, marrow transplantation between MLC-reactive individuals may become feasible. | [
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|
PMID:12849 | Looking both ways. Presidential address delivered at British Institute of Radiology Annual Congress-9th April 1976. | The address looks backward over the progress made in the techniques of radiology--both diagnosis and therapy--over the past 30 years and forward to the possibilities which lie ahead. It draws attention to the continuing need for basic research as the source from which practical advances spring, illustrating this from the development of radiosensitizing drugs. Finally, it emphasized the importance of the Institute as an interdisciplinary forum in the present era of rapid technological advance. | Looking both ways. Presidential address delivered at British Institute of Radiology Annual Congress-9th April 1976. The address looks backward over the progress made in the techniques of radiology--both diagnosis and therapy--over the past 30 years and forward to the possibilities which lie ahead. It draws attention to the continuing need for basic research as the source from which practical advances spring, illustrating this from the development of radiosensitizing drugs. Finally, it emphasized the importance of the Institute as an interdisciplinary forum in the present era of rapid technological advance. | [
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|
PMID:12850 | Atenolol, methyldopa, and chlorthalidone in moderate hypertension. | Combined treatment with low doses of different drugs is widely used for moderate hypertension. The effects of atenolol and methyldopa at two dose levels and in combination at the lower doses were studied in patients with moderate hypertension on continuous treatment with moderate hypertension on continuous treatment with chlorthalidone. The mean reduction in standing blood pressures obtained with atenolol 150 and 300 mg/day was about 27/17 mm Hg and with methyldopa 750 and 1500 mg/day about 28/14 mm Hg. Combined treatment with atenolol 150 mg/day and methyldopa 750 mg/day for four weeks resulted in a reduction of 38/25 mm Hg. No difference was observed between the two doses of methyldopa. The lower dose of atenolol was better than the lower dose of methyldopa in reducing lying and standing diastolic blood pressures. These findings show that in patients on continuous treatment with chlorthalidone the addition of atenolol alone or methyldopa alone or of atenolol and methyldopa in combination is effective in the treatment of moderate hypertension. | Atenolol, methyldopa, and chlorthalidone in moderate hypertension. Combined treatment with low doses of different drugs is widely used for moderate hypertension. The effects of atenolol and methyldopa at two dose levels and in combination at the lower doses were studied in patients with moderate hypertension on continuous treatment with moderate hypertension on continuous treatment with chlorthalidone. The mean reduction in standing blood pressures obtained with atenolol 150 and 300 mg/day was about 27/17 mm Hg and with methyldopa 750 and 1500 mg/day about 28/14 mm Hg. Combined treatment with atenolol 150 mg/day and methyldopa 750 mg/day for four weeks resulted in a reduction of 38/25 mm Hg. No difference was observed between the two doses of methyldopa. The lower dose of atenolol was better than the lower dose of methyldopa in reducing lying and standing diastolic blood pressures. These findings show that in patients on continuous treatment with chlorthalidone the addition of atenolol alone or methyldopa alone or of atenolol and methyldopa in combination is effective in the treatment of moderate hypertension. | [
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|
PMID:12851 | Tetracycline resistance in pneumococci and group A streptococci. Report of an ad-hoc study group on antibiotic resistance. | In a nationwide survey in the spring of 1975 into the prevalence of tetracycline resistance among pneumoccoci and group A streptococci isolates, 21 laboratories reported the sensitivity of isolates and details of the patients. Altogether 13% of the 1528 pneumococci isolated were resistant to tetracycline, but there were wide geographical variations. Thirty-six per cent of the 1515 streptococci isolated were resistant, and again there was considerable geographical variation. A high level of resistance in one organism did not correlate with a high level in the other. For both organisms resistance was commoner among inpatients and those aged 50 or over. Tetracycline should probably not be the drug of choice in penicillin-sensitive patients with group A streptococcal infections, but geographical variations were so wide that decisions on treatment are best made on the basis of local survey data. | Tetracycline resistance in pneumococci and group A streptococci. Report of an ad-hoc study group on antibiotic resistance. In a nationwide survey in the spring of 1975 into the prevalence of tetracycline resistance among pneumoccoci and group A streptococci isolates, 21 laboratories reported the sensitivity of isolates and details of the patients. Altogether 13% of the 1528 pneumococci isolated were resistant to tetracycline, but there were wide geographical variations. Thirty-six per cent of the 1515 streptococci isolated were resistant, and again there was considerable geographical variation. A high level of resistance in one organism did not correlate with a high level in the other. For both organisms resistance was commoner among inpatients and those aged 50 or over. Tetracycline should probably not be the drug of choice in penicillin-sensitive patients with group A streptococcal infections, but geographical variations were so wide that decisions on treatment are best made on the basis of local survey data. | [
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|
PMID:12856 | GABA and glycine transport in frog CNS: high affinity uptake and potassium-evoked release in vitro. | Slices of frog cerebrum, optic tectum, medulla and spinal cord rapidly accumulate [3H]GABA and [3H]glycine from the surrounding medium so that after 10 min tissue:medium ratios as high as 113 for GABA (optic tectum) and 18.5 for glycine (medulla) may be achieved. Kinetic analysis revealed two distinct saturable uptake systems for each amino acid in the 4 CNS areas. The high affinity systems (apparent Km: 9-22 muM for GABA; 5-35 muM for glycine) required sodium ions in the medium and were relatively substrate specific. Significant release of [3H]GABA and [3H]glycine, but not of L-[3H]leucine, was evoked by exposure to medium containing potassium ions in a concentration of 40 mM. The process of release was calcium-dependent. The importance of these results with regard to the roles of GABA and glycine as neurotransmitters in both spinal and supraspinal levels of the amphibian neuraxis is discussed. | GABA and glycine transport in frog CNS: high affinity uptake and potassium-evoked release in vitro. Slices of frog cerebrum, optic tectum, medulla and spinal cord rapidly accumulate [3H]GABA and [3H]glycine from the surrounding medium so that after 10 min tissue:medium ratios as high as 113 for GABA (optic tectum) and 18.5 for glycine (medulla) may be achieved. Kinetic analysis revealed two distinct saturable uptake systems for each amino acid in the 4 CNS areas. The high affinity systems (apparent Km: 9-22 muM for GABA; 5-35 muM for glycine) required sodium ions in the medium and were relatively substrate specific. Significant release of [3H]GABA and [3H]glycine, but not of L-[3H]leucine, was evoked by exposure to medium containing potassium ions in a concentration of 40 mM. The process of release was calcium-dependent. The importance of these results with regard to the roles of GABA and glycine as neurotransmitters in both spinal and supraspinal levels of the amphibian neuraxis is discussed. | [
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|
PMID:12857 | Catecholamine turnover alterations in discrete areas of the median eminence of the 4- and 5-day cyclic rat. | Using quantitative microfluorimetry in combination with tyrosine hydroxylase inhibition (H44/68) the concentration and turnover of noradrenaline (NA) and dopamine (DA) was studied in the subependymal layer (SEL) and the medial (MPZ) and lateral palisade zone (LPZ) of the rat median eminence during the 4- and 5- day vaginal estrous cycle. Significant cyclic variations were only found in SEL and LPZ. The NA turnover in SEL was high on proestrous and low on all other days of the 4-day estrous cycle, whereas in the 5-day estrous cycle the NA turnover in SEL started to increase already on the second day of diestrous to reach a peak in the afternoon of proestrous. At that time also the NA concentrations in SEL were increased, although significantly only in the 5-day cyclic rats. The DA turnover in LPZ was low on proestrous and high on all other days in both 4-and 5-day cyclic rats. Apart from the median eminence cyclic variations in catecholamine metabolism were only found in the medial preoptic area, where NA turnover was high on proestrous and low on estrous-diestrous. The present findings give further support for the existence of a facilitatory noradrenergic and inhibitory dopaminergic mechanism in the control of gonadotrophin release. Furthermore, it is suggested that an acceleration of reticulo-hypothalamic NA turnover precedes the retardation of tubero-infundibular DA turnover found on proestrous and that the time lag between initial NA activation and subsequent DA inactivation is longer in the 5-than in the 4-day estrous cycle. | Catecholamine turnover alterations in discrete areas of the median eminence of the 4- and 5-day cyclic rat. Using quantitative microfluorimetry in combination with tyrosine hydroxylase inhibition (H44/68) the concentration and turnover of noradrenaline (NA) and dopamine (DA) was studied in the subependymal layer (SEL) and the medial (MPZ) and lateral palisade zone (LPZ) of the rat median eminence during the 4- and 5- day vaginal estrous cycle. Significant cyclic variations were only found in SEL and LPZ. The NA turnover in SEL was high on proestrous and low on all other days of the 4-day estrous cycle, whereas in the 5-day estrous cycle the NA turnover in SEL started to increase already on the second day of diestrous to reach a peak in the afternoon of proestrous. At that time also the NA concentrations in SEL were increased, although significantly only in the 5-day cyclic rats. The DA turnover in LPZ was low on proestrous and high on all other days in both 4-and 5-day cyclic rats. Apart from the median eminence cyclic variations in catecholamine metabolism were only found in the medial preoptic area, where NA turnover was high on proestrous and low on estrous-diestrous. The present findings give further support for the existence of a facilitatory noradrenergic and inhibitory dopaminergic mechanism in the control of gonadotrophin release. Furthermore, it is suggested that an acceleration of reticulo-hypothalamic NA turnover precedes the retardation of tubero-infundibular DA turnover found on proestrous and that the time lag between initial NA activation and subsequent DA inactivation is longer in the 5-than in the 4-day estrous cycle. | [
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|
PMID:12862 | Cerebral carbohydrate metabolism during acute carbon monoxide intoxication. | The cerebral metabolic effects of 2.5, 5, 7.5, 10, 20, 30 and 60 min exposure to 1% CO were studied in lightly anesthetized rats by measurement of cerebral cortical contents of selected glycolytic and citric acid cylce intermediates, as well as tissue energy phosphates. The initial change in the glycolytic sequence occurred at 2.5 min with decreases in tissue glucose and glucose-6-phosphate and increases in fructose-1-6-diphosphate which indicated an activation of phosphofructokinase and hexokinase. The "crossover" pattern between glucose-6-phosphate and fructose-1,6-diphosphate was present at 5, 7.5 and 10 min, but not at 20, 30 and 60 min and thus confirmed previous observations that detection of phosphofructokinase activation in acute unifactorial cerebral hypoxia requires tissue study during the early phases of the experimental exposure. The initial activation of phosphofructokinase occurred in the absence of detectable changes in the tissue content of ATP, ADP, AMP or phosphocreatine and therefore suggested that an imbalance of tissue energy homeostasis is not a prerequisite for the activation of glycolysis in CO intoxication. One percent CO resulted in an increasing malate/oxaloacetate ratio at 5 min, followed by a decrease in alpha-ketoglutarate and aspartate at 7.5 min which suggested a shift in the aspartate aminotransferase reaction towards the replenishment of oxaloacetate removed via the malate dehydrogenase reaction. Subsequent increases in alpha-ketoglutarate at 10, 20, 30 and 60 min were associated with increases in alanine, indicating a contributing role for a secondary shift of the alanine aminotransferase reaction in the replenishment of alpha-ketoglutarate. A comparison of the CO induced changes in the glycolytic and citric acid cycle pathways with those seen in acute hypoxemia indicates no basic qualitative differences in the metabolic responses of brain tissue to the two conditions. | Cerebral carbohydrate metabolism during acute carbon monoxide intoxication. The cerebral metabolic effects of 2.5, 5, 7.5, 10, 20, 30 and 60 min exposure to 1% CO were studied in lightly anesthetized rats by measurement of cerebral cortical contents of selected glycolytic and citric acid cylce intermediates, as well as tissue energy phosphates. The initial change in the glycolytic sequence occurred at 2.5 min with decreases in tissue glucose and glucose-6-phosphate and increases in fructose-1-6-diphosphate which indicated an activation of phosphofructokinase and hexokinase. The "crossover" pattern between glucose-6-phosphate and fructose-1,6-diphosphate was present at 5, 7.5 and 10 min, but not at 20, 30 and 60 min and thus confirmed previous observations that detection of phosphofructokinase activation in acute unifactorial cerebral hypoxia requires tissue study during the early phases of the experimental exposure. The initial activation of phosphofructokinase occurred in the absence of detectable changes in the tissue content of ATP, ADP, AMP or phosphocreatine and therefore suggested that an imbalance of tissue energy homeostasis is not a prerequisite for the activation of glycolysis in CO intoxication. One percent CO resulted in an increasing malate/oxaloacetate ratio at 5 min, followed by a decrease in alpha-ketoglutarate and aspartate at 7.5 min which suggested a shift in the aspartate aminotransferase reaction towards the replenishment of oxaloacetate removed via the malate dehydrogenase reaction. Subsequent increases in alpha-ketoglutarate at 10, 20, 30 and 60 min were associated with increases in alanine, indicating a contributing role for a secondary shift of the alanine aminotransferase reaction in the replenishment of alpha-ketoglutarate. A comparison of the CO induced changes in the glycolytic and citric acid cycle pathways with those seen in acute hypoxemia indicates no basic qualitative differences in the metabolic responses of brain tissue to the two conditions. | [
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PMID:12863 | Isolation and characterization of a bacteriocin produced by Bacillus stearothermophilus strain NU-10. | Broth-grown cultures of Bacillus stearothermophilus strain NU-10 produce a bacteriocin which exerts lethal activity on other strains of the bacterium. Optimal production occurs during late maximum stationary phase of growth, at neutral pH, and 55-65 degrees C. The bacteriocin can be substantially purified by a combination of precipitations, centrifugations, and gel filtrations. The thermocin is composed of protein and carbohydrate. It is partially destroyed by proteolytic enzymes but is resistant to DNase, RNase, and various chemical treatments. The bacteriocin has a small molecular weight and exhibits considerable thermostability. | Isolation and characterization of a bacteriocin produced by Bacillus stearothermophilus strain NU-10. Broth-grown cultures of Bacillus stearothermophilus strain NU-10 produce a bacteriocin which exerts lethal activity on other strains of the bacterium. Optimal production occurs during late maximum stationary phase of growth, at neutral pH, and 55-65 degrees C. The bacteriocin can be substantially purified by a combination of precipitations, centrifugations, and gel filtrations. The thermocin is composed of protein and carbohydrate. It is partially destroyed by proteolytic enzymes but is resistant to DNase, RNase, and various chemical treatments. The bacteriocin has a small molecular weight and exhibits considerable thermostability. | [
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|
PMID:12864 | A radioimmunoassay method for 1-beta-D-arabinofuranosyluracil using antibodies directed against 1-beta-D-arabinofuranosylcytosine. | Above pH 7.0 1-beta-D-arabinofuranosyluracil (ara-U) shows marked pH-dependent cross-reactivity with antibodies directed towards 1-beta-D-arabinofuranosylcytosine. Since this peculiar phenomenon has not been observed with other nucleosides and nucleotides thus far tested, it is probably the result of base-catalyzed tautomerism of ara-U to its enolic form which renders it more structurally similar to 1-beta-D-arabinofuranosylcytosine. By performing the radioimmunoassay at both pH 6.2 and 8.6 we could determine 1-beta-D-arabinofuranosylcytosine and ara-U simultaneously. This method for ara-U assay is simple, fairly reliable, and applicable to blood level studies. | A radioimmunoassay method for 1-beta-D-arabinofuranosyluracil using antibodies directed against 1-beta-D-arabinofuranosylcytosine. Above pH 7.0 1-beta-D-arabinofuranosyluracil (ara-U) shows marked pH-dependent cross-reactivity with antibodies directed towards 1-beta-D-arabinofuranosylcytosine. Since this peculiar phenomenon has not been observed with other nucleosides and nucleotides thus far tested, it is probably the result of base-catalyzed tautomerism of ara-U to its enolic form which renders it more structurally similar to 1-beta-D-arabinofuranosylcytosine. By performing the radioimmunoassay at both pH 6.2 and 8.6 we could determine 1-beta-D-arabinofuranosylcytosine and ara-U simultaneously. This method for ara-U assay is simple, fairly reliable, and applicable to blood level studies. | [
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|
PMID:12865 | Dissociation of 5-fluorouracil uptake from intracellular pH in Walker 256 carcinosarcoma. | The influence of intracellular pH (pHi) upon 5-fluorouracil (5-FU) uptake has been studied in slices of Walker 256 carcinosarcoma and rat liver. Alteration of pHi was achieved by the addition of either glucose alone or together with oxamic acid to the incubation medium. Results indicated that 5-FU uptake by the tumor slices was not dependent upon pHi, but was enhanced by the presence of glucose. Uptake of 5-FU by liver slices appeared to follow a pattern predictable from the pHi and the pK of the drug. | Dissociation of 5-fluorouracil uptake from intracellular pH in Walker 256 carcinosarcoma. The influence of intracellular pH (pHi) upon 5-fluorouracil (5-FU) uptake has been studied in slices of Walker 256 carcinosarcoma and rat liver. Alteration of pHi was achieved by the addition of either glucose alone or together with oxamic acid to the incubation medium. Results indicated that 5-FU uptake by the tumor slices was not dependent upon pHi, but was enhanced by the presence of glucose. Uptake of 5-FU by liver slices appeared to follow a pattern predictable from the pHi and the pK of the drug. | [
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|
PMID:12866 | New sugars from antigenic lipopolysaccharides of bacteria: identification and synthesis of 3-O-[(R)-1-carboxyethyl]-L-rhamnose, an acidic component of Shigella dysenteriae type 5 lipopolysaccharide. | A new acidic sugar, 3-O-[(R)-1-carboxyethyl]-L-rhamnose (1), has been identified as a constituent of the O-antigenic lipopolysaccharide of Sh. dysenteriae type 5. The structure of 1 has been established by physico-chemical methods and by synthesis. Alkylation of methyl 2,5-di-O-benzyl-alpha-L-rhamnofuranoside (6) with (S)- or (R)-2-chloropropionic acids, followed by removal of the protecting groups, afforded 3-O-[(R)-1-carboxyethyl]-L-rhamnose (9) and 3-O-[(S)-1-carboxyethyl]-L-rhamnose (10), respectively. The properties of 1 coincide with those of 9. | New sugars from antigenic lipopolysaccharides of bacteria: identification and synthesis of 3-O-[(R)-1-carboxyethyl]-L-rhamnose, an acidic component of Shigella dysenteriae type 5 lipopolysaccharide. A new acidic sugar, 3-O-[(R)-1-carboxyethyl]-L-rhamnose (1), has been identified as a constituent of the O-antigenic lipopolysaccharide of Sh. dysenteriae type 5. The structure of 1 has been established by physico-chemical methods and by synthesis. Alkylation of methyl 2,5-di-O-benzyl-alpha-L-rhamnofuranoside (6) with (S)- or (R)-2-chloropropionic acids, followed by removal of the protecting groups, afforded 3-O-[(R)-1-carboxyethyl]-L-rhamnose (9) and 3-O-[(S)-1-carboxyethyl]-L-rhamnose (10), respectively. The properties of 1 coincide with those of 9. | [
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|
PMID:12867 | Analysis of the inotropic: chronotropic selectivity of dobutamine and dopamine in anaethetised dogs and guinea-pig isolated atria. | The previously reported in vivo inotropic selectivity of dobutamine and dopamine compared with isoprenaline has been demonstrated in anaesthetised bivagotamised open chest dogs. Responses of heart rate, right ventricular tension, left ventricular dP/dtmax, and blood pressure were measured. Compared with isoprenaline, dobutamine and dopamine were 1.8 and 2.4 times more active in increasing cardiac contractility than rate. The inotropic selectivity of dopamine but not that of dobutamine was abolished by pretreatment of dogs with syrosingopine. In guinea-pig isolated atria, isoprenaline, dobutamine, and dopamine were all slightly rate selective although this was less for dopamine. In atria incubated with phenoxybenzamine from guinea-pigs pretreated with reserpine only the dopamine dose-response curves were displaced to the right indicating a considerable indirect sympathomimetic component. The in vivo inotropic selectivity of dopamine could therefore be explained on the basis of this indirect activity being manifested at lower doses in the myocardium where the stores of catecholamines are more abundant than at the sinoatrial node. However, it is concluded that the inotropic selectivity of dobutamine seen in vivo is not due to indirect activity, reflex effects, or to a difference in the beta-adrenoceptors mediating the rate and tension responses of the heart. Possible alternative explanations are discussed. | Analysis of the inotropic: chronotropic selectivity of dobutamine and dopamine in anaethetised dogs and guinea-pig isolated atria. The previously reported in vivo inotropic selectivity of dobutamine and dopamine compared with isoprenaline has been demonstrated in anaesthetised bivagotamised open chest dogs. Responses of heart rate, right ventricular tension, left ventricular dP/dtmax, and blood pressure were measured. Compared with isoprenaline, dobutamine and dopamine were 1.8 and 2.4 times more active in increasing cardiac contractility than rate. The inotropic selectivity of dopamine but not that of dobutamine was abolished by pretreatment of dogs with syrosingopine. In guinea-pig isolated atria, isoprenaline, dobutamine, and dopamine were all slightly rate selective although this was less for dopamine. In atria incubated with phenoxybenzamine from guinea-pigs pretreated with reserpine only the dopamine dose-response curves were displaced to the right indicating a considerable indirect sympathomimetic component. The in vivo inotropic selectivity of dopamine could therefore be explained on the basis of this indirect activity being manifested at lower doses in the myocardium where the stores of catecholamines are more abundant than at the sinoatrial node. However, it is concluded that the inotropic selectivity of dobutamine seen in vivo is not due to indirect activity, reflex effects, or to a difference in the beta-adrenoceptors mediating the rate and tension responses of the heart. Possible alternative explanations are discussed. | [
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|
PMID:12869 | The effect of fixation conditions on the ultrastructural appearance of gastrin cell granules in the rat gastric pyloric antrum. | The ultrastructural appearance of gastrin cell (G cell) granules was studied after different fixation procedures. When the pH of prefixation was varied there was greater preservation of the electron density of granule cores after acidic (pH 5.0 and 6.0) than after neutral or alkaline (pH 7.0 and 8.0) prefixation. Increasing duration of prefixation at pH 7.3 resulted in progressive loss of electron density of the granule core with swelling and occasional rupture of the limiting membrane. In tissues where most granules had been rendered electron lucent by fixation, those granules remaining dense cored were preferentially located close to the Golgi zone. These findings indicate that the electron density of G cell granules is profoundly affected by conditions of fixation, and that immature granules are more resistant to loss of core density than mature granules. They also suggest that the gastrin granule in vivo, like other polypeptide granules, may have a "solid", osmotically inactive core. | The effect of fixation conditions on the ultrastructural appearance of gastrin cell granules in the rat gastric pyloric antrum. The ultrastructural appearance of gastrin cell (G cell) granules was studied after different fixation procedures. When the pH of prefixation was varied there was greater preservation of the electron density of granule cores after acidic (pH 5.0 and 6.0) than after neutral or alkaline (pH 7.0 and 8.0) prefixation. Increasing duration of prefixation at pH 7.3 resulted in progressive loss of electron density of the granule core with swelling and occasional rupture of the limiting membrane. In tissues where most granules had been rendered electron lucent by fixation, those granules remaining dense cored were preferentially located close to the Golgi zone. These findings indicate that the electron density of G cell granules is profoundly affected by conditions of fixation, and that immature granules are more resistant to loss of core density than mature granules. They also suggest that the gastrin granule in vivo, like other polypeptide granules, may have a "solid", osmotically inactive core. | [
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|
PMID:12870 | Stable mutants of mammalian cells that overproduce the first three enzymes of pyrimidine nucleotide biosynthesis. | Upon exposure to 0.1 mM N-phosphonacetyl-L-aspartate (PALA), a transition state analog inhibitor of aspartate transcarbamylase, most cells of a simian virus 40 (SV40)-transformed Syrian hamster line are killed within a few days, but resistant mutants form spontaneously with frequency 2-5 X 10(-5) in a stochastic process not dependent upon the presence of the inhibitor. The resistant phenotype is stable for many months in the absence of PALA. Other cell lines also give resistant mutants, but with substantially lower frequencies. Serial selection with PALA at concentrations up to 25 mM has yielded clones with more than 100 times the original aspartate transcarbamylase activity. The activities of carbamyl-P synthetase and dihydroorotase, which co-purify with aspartate transcarbamylase as a three-enzyme complex, increase in parallel with aspartate transcarbamylase activity in each resistant clone tested, but there is no substantial change in the activities of the last three enzymes of the de novo pathway, which are not in this complex. In each of the three resistant clones tested, there is an increase in the number of aspartate transcarbamylase active sites, determined by titration with 3H-PALA, which closely parallels the increase in enzyme activity. In one resistant clone tested, there is no change in the Ki for PALA or the Km for carbamyl-P. The only mechanism detected for achieving resistance to PALA is an increase in the steady state amount of the three enzyme complex. | Stable mutants of mammalian cells that overproduce the first three enzymes of pyrimidine nucleotide biosynthesis. Upon exposure to 0.1 mM N-phosphonacetyl-L-aspartate (PALA), a transition state analog inhibitor of aspartate transcarbamylase, most cells of a simian virus 40 (SV40)-transformed Syrian hamster line are killed within a few days, but resistant mutants form spontaneously with frequency 2-5 X 10(-5) in a stochastic process not dependent upon the presence of the inhibitor. The resistant phenotype is stable for many months in the absence of PALA. Other cell lines also give resistant mutants, but with substantially lower frequencies. Serial selection with PALA at concentrations up to 25 mM has yielded clones with more than 100 times the original aspartate transcarbamylase activity. The activities of carbamyl-P synthetase and dihydroorotase, which co-purify with aspartate transcarbamylase as a three-enzyme complex, increase in parallel with aspartate transcarbamylase activity in each resistant clone tested, but there is no substantial change in the activities of the last three enzymes of the de novo pathway, which are not in this complex. In each of the three resistant clones tested, there is an increase in the number of aspartate transcarbamylase active sites, determined by titration with 3H-PALA, which closely parallels the increase in enzyme activity. In one resistant clone tested, there is no change in the Ki for PALA or the Km for carbamyl-P. The only mechanism detected for achieving resistance to PALA is an increase in the steady state amount of the three enzyme complex. | [
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|
PMID:12875 | Interactions of various 19-nor steroids with human placental microsomal cytochrome P-450 (P-450hpm). | Each of seven 19-nor steroids exhibited the capacity to facilitate the binding of carbon monoxide (CO) to human placental microsomal cytochrome P-450 although quantitative differences were shown to exist. In every case the facilitation was antagonized by androstenedione. 19-Norandrostenedione produced the most pronounced effect followed by 19-nortestosterone, nandrolone decanoate, norethandrolone, norgestrel, norethynodrel and norethindrone in that order. All steroids investigated produced typical type I binding spectra when added to placental microsomes. Scatched plots also indicated binding of each steroid to two sites--a high-affinity, low-capacity binding site and a low-affinity, high-capacity binding site. Correlations between affinity for either site and capacity to facilitate binding of CO to the cytochrome were not observed nor were there good correlations between maximal absorbance differences (approximately390-420 nm) producible and facilitation capacity. It was therefore concluded that no definitive relationships existed between facilitation capacity and qualitative or quantitative aspects of the steroid-binding spectra. The capacity to facilitate CO binding appeared to reside in the absence of a chemical group substituted at the 10 position on molecules of androgenic steroids since all investigated steroids possessing 10-methyl or other 10-substituted groups either had no effect on the CO-binding spectrum or caused a displacement of CO from ferrous heme. In contrast, all steroids studied that lacked a substitution at C-10 (19-nor steroids) produced a facilitating effect on heme-ligand binding. | Interactions of various 19-nor steroids with human placental microsomal cytochrome P-450 (P-450hpm). Each of seven 19-nor steroids exhibited the capacity to facilitate the binding of carbon monoxide (CO) to human placental microsomal cytochrome P-450 although quantitative differences were shown to exist. In every case the facilitation was antagonized by androstenedione. 19-Norandrostenedione produced the most pronounced effect followed by 19-nortestosterone, nandrolone decanoate, norethandrolone, norgestrel, norethynodrel and norethindrone in that order. All steroids investigated produced typical type I binding spectra when added to placental microsomes. Scatched plots also indicated binding of each steroid to two sites--a high-affinity, low-capacity binding site and a low-affinity, high-capacity binding site. Correlations between affinity for either site and capacity to facilitate binding of CO to the cytochrome were not observed nor were there good correlations between maximal absorbance differences (approximately390-420 nm) producible and facilitation capacity. It was therefore concluded that no definitive relationships existed between facilitation capacity and qualitative or quantitative aspects of the steroid-binding spectra. The capacity to facilitate CO binding appeared to reside in the absence of a chemical group substituted at the 10 position on molecules of androgenic steroids since all investigated steroids possessing 10-methyl or other 10-substituted groups either had no effect on the CO-binding spectrum or caused a displacement of CO from ferrous heme. In contrast, all steroids studied that lacked a substitution at C-10 (19-nor steroids) produced a facilitating effect on heme-ligand binding. | [
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|
PMID:12876 | Fatty acids diffusion in lecithin multilayers: hydration and PH effects. | The diffusion of the sodium salt of monocarboxylic fatty acids, from formate to stearate, has been studied as a function of water content and pH in lecithin--water lamellar phases. Evolution of the diffusion coefficients with increasing chain length reflects the different localizations of fatty acids in the system. From formate to butyrate, which are mainly restricted to the hydrophilic layer of the phase, diffusion rates decrease rapidly. From butyrate to stearate, fatty acids (anchored at the hydrophilic--lipophilic interface) undergo lateral diffusion and then the decrease of D with increasing chain length is much slower. The diffusion of stereate is already comparable to the diffusion of the lecithin molecule itself. The diffusion rates strongly depend upon phase hydration and pH: it is shown that both parameters control the fatty acid ionization. The variations in diffusion rates observed may be ascribed to the fact that, depending upon their state of ionization, fatty acids assume a different localization and therefore experience different interactions in the lamellar system. | Fatty acids diffusion in lecithin multilayers: hydration and PH effects. The diffusion of the sodium salt of monocarboxylic fatty acids, from formate to stearate, has been studied as a function of water content and pH in lecithin--water lamellar phases. Evolution of the diffusion coefficients with increasing chain length reflects the different localizations of fatty acids in the system. From formate to butyrate, which are mainly restricted to the hydrophilic layer of the phase, diffusion rates decrease rapidly. From butyrate to stearate, fatty acids (anchored at the hydrophilic--lipophilic interface) undergo lateral diffusion and then the decrease of D with increasing chain length is much slower. The diffusion of stereate is already comparable to the diffusion of the lecithin molecule itself. The diffusion rates strongly depend upon phase hydration and pH: it is shown that both parameters control the fatty acid ionization. The variations in diffusion rates observed may be ascribed to the fact that, depending upon their state of ionization, fatty acids assume a different localization and therefore experience different interactions in the lamellar system. | [
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|
PMID:12878 | [Hydrochloric acid secretion of fetal rat gastric mucosa]. | In Rat, spontaneous secretion of hydrochloric acid by gastric mucosa takes place before birth. From day 20 of gestation until birth, the pH of gastric content markedly decreases, reaching 3 pH-units in newborns. During this period, Cl- concentration in gastric juice increases, while p-CO2 remains constant. | [Hydrochloric acid secretion of fetal rat gastric mucosa]. In Rat, spontaneous secretion of hydrochloric acid by gastric mucosa takes place before birth. From day 20 of gestation until birth, the pH of gastric content markedly decreases, reaching 3 pH-units in newborns. During this period, Cl- concentration in gastric juice increases, while p-CO2 remains constant. | [
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|
PMID:12879 | [Multiplicity of beta lactamases: a problem of isoenzymes]. | Analytical isoelectric focusing of beta lactamases is a very sensitive and powerful technique which generally shows a number of satellites near the main enzymatic spike. By this technique we studied two bacterial groups known to produce different beta lactamases, but only one by germ. Analytical isoelectric focusing showed that all bacteria from the same group produce the same satellite system which differs only in relative activity. | [Multiplicity of beta lactamases: a problem of isoenzymes]. Analytical isoelectric focusing of beta lactamases is a very sensitive and powerful technique which generally shows a number of satellites near the main enzymatic spike. By this technique we studied two bacterial groups known to produce different beta lactamases, but only one by germ. Analytical isoelectric focusing showed that all bacteria from the same group produce the same satellite system which differs only in relative activity. | [
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|
PMID:12880 | Hemodynamic effects of labetalol, an alpha and beta adrenergic blocking agent, in hypertensive subjects. | Labetalol was administered to six hypertensive subjects in increasing doses for seven days. A decrease in both supine and standing arterial pressure and heart rate was observed with no change in cardiac output and few side effects. Exercise tolerance was unaltered by the drug, but the heart rate and arterial pressure response to exercise were significantly blunted. The infusion rate of isoproterenol required to produce tachycardia was increased sevenfold by 800 mg/day labetalol and tenfold by 1600 mg/day. More than twice the control dose of phenylephrine was required during labetalol therapy to produce a rise in diastolic arterial pressure reflex tachycardia to amyl nitrite-induced hypotension was attenuated. These studies indingina pectoris. | Hemodynamic effects of labetalol, an alpha and beta adrenergic blocking agent, in hypertensive subjects. Labetalol was administered to six hypertensive subjects in increasing doses for seven days. A decrease in both supine and standing arterial pressure and heart rate was observed with no change in cardiac output and few side effects. Exercise tolerance was unaltered by the drug, but the heart rate and arterial pressure response to exercise were significantly blunted. The infusion rate of isoproterenol required to produce tachycardia was increased sevenfold by 800 mg/day labetalol and tenfold by 1600 mg/day. More than twice the control dose of phenylephrine was required during labetalol therapy to produce a rise in diastolic arterial pressure reflex tachycardia to amyl nitrite-induced hypotension was attenuated. These studies indingina pectoris. | [
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|
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