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PMID:19360
|
Activation of botulinum toxins in the absence of nicking.
|
The derivative toxins purified from cultures of proteolytic strains of Clostridium botulinum types A and F were found to have been only partially nicked but were fully activated. Trypsinization of C. botulinum type B derivative toxin at pH 6.0 resulted in simultaneous activation and nicking, whereas at pH 4.5, activation preceded nicking. The toxin was split by trypsin at pH 6.0 into two fragments with molecular weights of 112, ooo and 57,000. The toxin contained at least three trypsin-sensitive peptide bonds, one of which was more sensitive than the others at pH 6.0. These results indicate that activation of botulinum toxins by trypsin or endogenous protease (s) is not a direct result of nicking.
|
Activation of botulinum toxins in the absence of nicking. The derivative toxins purified from cultures of proteolytic strains of Clostridium botulinum types A and F were found to have been only partially nicked but were fully activated. Trypsinization of C. botulinum type B derivative toxin at pH 6.0 resulted in simultaneous activation and nicking, whereas at pH 4.5, activation preceded nicking. The toxin was split by trypsin at pH 6.0 into two fragments with molecular weights of 112, ooo and 57,000. The toxin contained at least three trypsin-sensitive peptide bonds, one of which was more sensitive than the others at pH 6.0. These results indicate that activation of botulinum toxins by trypsin or endogenous protease (s) is not a direct result of nicking.
|
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] |
PMID:19362
|
Action of atropine on histamine-induced bronchoconstriction in asthmatic children. A pharmacocapnographic study.
|
In their earlier methodological model studies the authors confirmed the protective effect of atropine in inhalative acetylcholine provocation. In the present work the role of parasympatholysis is investigated in histamine-induced bronchospasm by the method. It was found that a protective effect was exerted in histamine provocation repeated 20 minutes after subcutaneous administration of atropine sulphate in a dose of 0.01 mg/kg. The protective effect proved independent of the individual histamine sensitivities of the patients. The initial value of the CO2 curve prior to provocation was not improved.
|
Action of atropine on histamine-induced bronchoconstriction in asthmatic children. A pharmacocapnographic study. In their earlier methodological model studies the authors confirmed the protective effect of atropine in inhalative acetylcholine provocation. In the present work the role of parasympatholysis is investigated in histamine-induced bronchospasm by the method. It was found that a protective effect was exerted in histamine provocation repeated 20 minutes after subcutaneous administration of atropine sulphate in a dose of 0.01 mg/kg. The protective effect proved independent of the individual histamine sensitivities of the patients. The initial value of the CO2 curve prior to provocation was not improved.
|
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] |
PMID:19364
|
Thin-layer and gas-liquid chromatographic procedures for the determination of perazine and its metabolites in human body fluids.
|
The quantitative determination of perazine, a neuroleptic drug, and its metabolites in body fluids is difficult in view of the low concentrations to be expected under therapeutic conditions as well as of the problem of convenient detectors. Different methods for extraction and measurement of perazine concentration in blood samples are discussed, with special consideration of partition coefficients and the properties of the chromatographic systems (thin-layer and gas-liquid chromatography). A new and simple method for rapid gas chromatographic determination of perazine is presented.
|
Thin-layer and gas-liquid chromatographic procedures for the determination of perazine and its metabolites in human body fluids. The quantitative determination of perazine, a neuroleptic drug, and its metabolites in body fluids is difficult in view of the low concentrations to be expected under therapeutic conditions as well as of the problem of convenient detectors. Different methods for extraction and measurement of perazine concentration in blood samples are discussed, with special consideration of partition coefficients and the properties of the chromatographic systems (thin-layer and gas-liquid chromatography). A new and simple method for rapid gas chromatographic determination of perazine is presented.
|
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] |
PMID:19365
|
A model for distinguishing between beta1-receptors which mediate a specific effect on the heart rate and those which mediate a positively inotropic effect.
|
The study was conducted in six healthy male volunteers aged between 20 and 30 years. Cardiac output was determined by means of the Swan-Ganz-thermodilution-method. A control-study was carried out, during which an isoproterenolinfusion with increasing doses was given. Fifty minutes after i.v. injection of a beta-receptor-blocker the hemodynamic parameters were measured again under increasing doses of isoproterenol until the block was overcome. This study procedure was performed twice in each subject at an interval of at least 14 days. For the one study 15 mg propranolol i.v. and for the other 0,5 mg mepindolol i.v., a new beta-receptor-blocker, were injected. After i.v. injection of propranolol the dose-response-relationship-curve for the heart-rate (HR) and stroke volume (SV) describes a definite shift to the right. After mepindolol the dose-effect curve for the heart rate describes a definite shift to the right, as seen with propranolol. In contrast, only a very slight shift can be seen in respect of the SV increase, i.e. the SV and HR curves dissociate under mepindolol. The results of our study indicate, that a distinction can be made with respect to the so-called beta 1-receptors between those mediating a specific effect on the heart-rate and those mediating a mainly positive inotropic effect.
|
A model for distinguishing between beta1-receptors which mediate a specific effect on the heart rate and those which mediate a positively inotropic effect. The study was conducted in six healthy male volunteers aged between 20 and 30 years. Cardiac output was determined by means of the Swan-Ganz-thermodilution-method. A control-study was carried out, during which an isoproterenolinfusion with increasing doses was given. Fifty minutes after i.v. injection of a beta-receptor-blocker the hemodynamic parameters were measured again under increasing doses of isoproterenol until the block was overcome. This study procedure was performed twice in each subject at an interval of at least 14 days. For the one study 15 mg propranolol i.v. and for the other 0,5 mg mepindolol i.v., a new beta-receptor-blocker, were injected. After i.v. injection of propranolol the dose-response-relationship-curve for the heart-rate (HR) and stroke volume (SV) describes a definite shift to the right. After mepindolol the dose-effect curve for the heart rate describes a definite shift to the right, as seen with propranolol. In contrast, only a very slight shift can be seen in respect of the SV increase, i.e. the SV and HR curves dissociate under mepindolol. The results of our study indicate, that a distinction can be made with respect to the so-called beta 1-receptors between those mediating a specific effect on the heart-rate and those mediating a mainly positive inotropic effect.
|
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] |
PMID:19366
|
Explanation of the observation of pancreatic ribonuclease activity at pH 4.5.
|
A recent conclusion that beef pancreas contained a molecular species of ribonuclease with intrinsically high activity at pH 4.5 has been found to be incorrect. The particular assay used in the earlier experiments gives anomalous results at acid pH in the presence of low concentrations of ions such as phosphate which was used during the fractionation. By turning to the more widely employed form of the perchloric acid precipitation assay, interference is avoided and the ribonuclease in beef pancreas is confirmed as consisting almost completely of the molecular species well-characterized as ribonuclease A. The clarification of the assay question permits a clear interpretation of the results of each step of the chromatographic purification procedure that led to the initial conclusion, including an artifact that arose when gel filtration was attempted with distilled water rather than with buffer.
|
Explanation of the observation of pancreatic ribonuclease activity at pH 4.5. A recent conclusion that beef pancreas contained a molecular species of ribonuclease with intrinsically high activity at pH 4.5 has been found to be incorrect. The particular assay used in the earlier experiments gives anomalous results at acid pH in the presence of low concentrations of ions such as phosphate which was used during the fractionation. By turning to the more widely employed form of the perchloric acid precipitation assay, interference is avoided and the ribonuclease in beef pancreas is confirmed as consisting almost completely of the molecular species well-characterized as ribonuclease A. The clarification of the assay question permits a clear interpretation of the results of each step of the chromatographic purification procedure that led to the initial conclusion, including an artifact that arose when gel filtration was attempted with distilled water rather than with buffer.
|
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] |
PMID:19367
|
Association-dissociation and denaturation behaviour of an oligomeric seed protein alpha-globulin of Sesamum indicum L. in acid and alkaline solutions.
|
The association-dissociation and denaturation behaviour of the major protein fraction, alpha-globulin of sesame seed (Sesamum indicum L.), in acid and alkaline solutions in the ranges of pH 4.2-1.5 and pH 7-12 have been studied. The results of gel filtration, fluorescence and viscosity measurements indicate dissociation and denaturation of the protein up to pH approximately 3. The difference spectrum in this region arises from a combination of dissociation, denaturation and charge effect on the chromophore. In still stronger acid solution, reassociation of the dissociated fraction takes place by hydrophobic interaction. In alkaline solution dissociation takes place around pH 8, and above pH 10 dissociation and denaturation proceed simultaneously as has been evidenced by sedimentation, fluorescence, spectral change, optical rotation and viscosity measurements. The phenolic group (pKInt=10.6) in the protein is abnormal and denaturation in alkaline solution is irreversible. Above pH 11.5 further dissociation of the protein takes place. Characteristic pH values of transition from 10.6-10.8 indicate that the transition of the protein involves a single step in alkaline solution.
|
Association-dissociation and denaturation behaviour of an oligomeric seed protein alpha-globulin of Sesamum indicum L. in acid and alkaline solutions. The association-dissociation and denaturation behaviour of the major protein fraction, alpha-globulin of sesame seed (Sesamum indicum L.), in acid and alkaline solutions in the ranges of pH 4.2-1.5 and pH 7-12 have been studied. The results of gel filtration, fluorescence and viscosity measurements indicate dissociation and denaturation of the protein up to pH approximately 3. The difference spectrum in this region arises from a combination of dissociation, denaturation and charge effect on the chromophore. In still stronger acid solution, reassociation of the dissociated fraction takes place by hydrophobic interaction. In alkaline solution dissociation takes place around pH 8, and above pH 10 dissociation and denaturation proceed simultaneously as has been evidenced by sedimentation, fluorescence, spectral change, optical rotation and viscosity measurements. The phenolic group (pKInt=10.6) in the protein is abnormal and denaturation in alkaline solution is irreversible. Above pH 11.5 further dissociation of the protein takes place. Characteristic pH values of transition from 10.6-10.8 indicate that the transition of the protein involves a single step in alkaline solution.
|
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-0.05426468700170517,
0.021890385076403618,
0.030176974833011627
] |
PMID:19368
|
Fluorescent labelling of 6-phosphogluconate dehydrogenase from Bacillus stearothermophilus.
|
The thermophilic 6-phosphogluconate dehydrogenase from Bacillus stearothermophilus was inhibited upon specific modification of the -SH group of cysteine residues by 7-chloro-4-nitrobenzo-2-oxa-1, 3-diazole (NBD-Cl) at pH 7.0. By using 20-100-fold molar excess of NBD-CL the reaction occurs slowly at pH 7.0 as a first order process. Partial protection from inactivation was observed when the substrate 6-phosphogluconate or the coenzyme NADP was added to the reaction mixture. Complete inactivation was achieved upon modification of 1.9 of the six cysteine residues per mole of enzyme, which corresponds to nearly one residue per enzyme subunit. Circular dichroism measurements suggest that the gross structure of the protein molecule is practically unchanged upon reaction of the enzyme with NBD-Cl. Melting profile experiments revealed a single transition occurring at about 65 degrees C. Analogously, the profile of intensity of the fluorescence emission at 520 nm of the enzyme-bound S-NBD groups versus temperature indicated a midpoint of transition near 65 degrees C. Since this melting temperature corresponds closely to that observed with the native enzyme, these results would indicate that the molecular organizations of the native and modified enzyme are similar and stabilized by similar interactions within the polypeptide chain.
|
Fluorescent labelling of 6-phosphogluconate dehydrogenase from Bacillus stearothermophilus. The thermophilic 6-phosphogluconate dehydrogenase from Bacillus stearothermophilus was inhibited upon specific modification of the -SH group of cysteine residues by 7-chloro-4-nitrobenzo-2-oxa-1, 3-diazole (NBD-Cl) at pH 7.0. By using 20-100-fold molar excess of NBD-CL the reaction occurs slowly at pH 7.0 as a first order process. Partial protection from inactivation was observed when the substrate 6-phosphogluconate or the coenzyme NADP was added to the reaction mixture. Complete inactivation was achieved upon modification of 1.9 of the six cysteine residues per mole of enzyme, which corresponds to nearly one residue per enzyme subunit. Circular dichroism measurements suggest that the gross structure of the protein molecule is practically unchanged upon reaction of the enzyme with NBD-Cl. Melting profile experiments revealed a single transition occurring at about 65 degrees C. Analogously, the profile of intensity of the fluorescence emission at 520 nm of the enzyme-bound S-NBD groups versus temperature indicated a midpoint of transition near 65 degrees C. Since this melting temperature corresponds closely to that observed with the native enzyme, these results would indicate that the molecular organizations of the native and modified enzyme are similar and stabilized by similar interactions within the polypeptide chain.
|
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0.06439074873924255,
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] |
PMID:19369
|
The possible role of dopamine in phenothiazine-induced hypothermia in rats: an application to DA hypothesis of schizophrenia.
|
Hypothermic effects of d-Amphetamine, chlorpromazine, a variety of other phenothiazines, ET495 and haloperidol in rats at 4 degrees C were measured separately and in combination. All the drugs produced some hypothermia. Among the phenothiazines, degree of hypothermia induced was found to be correlated with relative effectiveness of the drug as an antipsychotic agent. Hypothermic effects of each of the phenothiazines in combination with d-Amphetadrugs as an antipsychotic agent. Hypothermic effects of each of the phenothiazines in combination with d-Amphetamine was greater than for either drug alone. Hypothermic effects of the combination CPZ with Amphetamine was potentiated by haloperidol but blocked by ET495. The evidence supports a model of neuronal feedback loops either within the central DA mesolimbic pathway or between the mesolimbic and nigrostriatal DA systems. The establishment of interdependency between antipsychotic and hypothermic effects of phenothiazines offers promise not only to a greater understanding of the mechanisms underlying these effects, but the possibility of an objective test for screening new materials for antipsychotic effectiveness.
|
The possible role of dopamine in phenothiazine-induced hypothermia in rats: an application to DA hypothesis of schizophrenia. Hypothermic effects of d-Amphetamine, chlorpromazine, a variety of other phenothiazines, ET495 and haloperidol in rats at 4 degrees C were measured separately and in combination. All the drugs produced some hypothermia. Among the phenothiazines, degree of hypothermia induced was found to be correlated with relative effectiveness of the drug as an antipsychotic agent. Hypothermic effects of each of the phenothiazines in combination with d-Amphetadrugs as an antipsychotic agent. Hypothermic effects of each of the phenothiazines in combination with d-Amphetamine was greater than for either drug alone. Hypothermic effects of the combination CPZ with Amphetamine was potentiated by haloperidol but blocked by ET495. The evidence supports a model of neuronal feedback loops either within the central DA mesolimbic pathway or between the mesolimbic and nigrostriatal DA systems. The establishment of interdependency between antipsychotic and hypothermic effects of phenothiazines offers promise not only to a greater understanding of the mechanisms underlying these effects, but the possibility of an objective test for screening new materials for antipsychotic effectiveness.
|
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] |
PMID:19370
|
WIN 27,147-2 in the treatment of depression. An uncontrolled clinical study.
|
An uncontrolled clinical study with WIN 27,147-2 was conducted with 10 hospitalized depressed psychiatric patients. There was statistically significant improvement in the total scores of the HAM-D, BPRS and Zung; in the scores of all the factors of the HAM-D and Zung; in the scores of the anxiety/depression and activation factors of the BPRS, and in the scores of 6 of the 18 items of the BPRS. Judged by clinical global impression, 9 of the 10 patients were very much improved and 1 patient much improved. The most frequently occurring adverse effects were dry mouth, sweating, drowsiness and insomnia.
|
WIN 27,147-2 in the treatment of depression. An uncontrolled clinical study. An uncontrolled clinical study with WIN 27,147-2 was conducted with 10 hospitalized depressed psychiatric patients. There was statistically significant improvement in the total scores of the HAM-D, BPRS and Zung; in the scores of all the factors of the HAM-D and Zung; in the scores of the anxiety/depression and activation factors of the BPRS, and in the scores of 6 of the 18 items of the BPRS. Judged by clinical global impression, 9 of the 10 patients were very much improved and 1 patient much improved. The most frequently occurring adverse effects were dry mouth, sweating, drowsiness and insomnia.
|
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0.043819405138492584,
-0.02609233371913433,
0.09531056135892868,
0.01590169221162796
] |
PMID:19375
|
Some properties of hemoglobin Gun Hill.
|
Hb Gun Hill has been found in an asymptomatic black female living in Alabama; neither her parents nor her two siblings carry the variant. The deletion of five amino acid residues in the beta chain of Hb Gun Hill (alpha2beta2 91-95 deleted) causes this variant to have a high oxygen affinity, an interaction coefficient of unity and an absence of the Bohr effect. The rate of oxidation of liganded Hb Gun Hill by the ferricyanide ion follows first-order kinetics. Hb Gun Hill is to a great extent dissociated into dimers over a wide range of pH values.
|
Some properties of hemoglobin Gun Hill. Hb Gun Hill has been found in an asymptomatic black female living in Alabama; neither her parents nor her two siblings carry the variant. The deletion of five amino acid residues in the beta chain of Hb Gun Hill (alpha2beta2 91-95 deleted) causes this variant to have a high oxygen affinity, an interaction coefficient of unity and an absence of the Bohr effect. The rate of oxidation of liganded Hb Gun Hill by the ferricyanide ion follows first-order kinetics. Hb Gun Hill is to a great extent dissociated into dimers over a wide range of pH values.
|
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] |
PMID:19376
|
A test tube method for quantitation of hemoglobin A2 using DE 52 cellulose.
|
A test tube method for quantitation of Hb A2 which is an adaption of the microcolumn chromatographic method is described. The method uses microangular DEAE cellulose (DE 52, microgranular and preswollen, Whatman Inc.) equilibrated with a 0.2 M glycine-0.1% KCN solution, pH 7.25. Hemoglobin A and F become bound to the resin while Hb A2 is in supernatant fraction allowing its quantitation. The method is simple, rapid, inexpensive and accurate, and allows one technician to determine the level of Hb A2 in at least 50 samples a day. The method can be used with whole blood, hemolysates and blood collected on filter paper.
|
A test tube method for quantitation of hemoglobin A2 using DE 52 cellulose. A test tube method for quantitation of Hb A2 which is an adaption of the microcolumn chromatographic method is described. The method uses microangular DEAE cellulose (DE 52, microgranular and preswollen, Whatman Inc.) equilibrated with a 0.2 M glycine-0.1% KCN solution, pH 7.25. Hemoglobin A and F become bound to the resin while Hb A2 is in supernatant fraction allowing its quantitation. The method is simple, rapid, inexpensive and accurate, and allows one technician to determine the level of Hb A2 in at least 50 samples a day. The method can be used with whole blood, hemolysates and blood collected on filter paper.
|
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] |
PMID:19373
|
The effect of different endotracheal suction procedures on arterial blood gases in a controlled experimental model.
|
In an anesthetized hypoxemic animal model, 15 seconds of endotracheal suctioning, using a suction pressure of --170 mm. Hg and endotracheal tube to suction catheter ratio of 1.87 to 1, produced a 13 mm. Hg fall in arterial oxygen tension. Oxygen tension did not return to control level even at 5 minutes after suctioning. Giving 100 per cent oxygen before suctioning prevented suction-induced hypoxemia during and immediately after suctioning, but at 5 minutes after suctioning, oxygen tension fell below control levels. Mechanical lung hyperinflation with room air after suctioning quickly raised arterial oxygen tension above control levels. When mechanical ventilation using 100 per cent oxygen was maintained before, during, and after the suction procedure, arterial oxygen tension remained elevated at all times.
|
The effect of different endotracheal suction procedures on arterial blood gases in a controlled experimental model. In an anesthetized hypoxemic animal model, 15 seconds of endotracheal suctioning, using a suction pressure of --170 mm. Hg and endotracheal tube to suction catheter ratio of 1.87 to 1, produced a 13 mm. Hg fall in arterial oxygen tension. Oxygen tension did not return to control level even at 5 minutes after suctioning. Giving 100 per cent oxygen before suctioning prevented suction-induced hypoxemia during and immediately after suctioning, but at 5 minutes after suctioning, oxygen tension fell below control levels. Mechanical lung hyperinflation with room air after suctioning quickly raised arterial oxygen tension above control levels. When mechanical ventilation using 100 per cent oxygen was maintained before, during, and after the suction procedure, arterial oxygen tension remained elevated at all times.
|
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] |
PMID:19377
|
Isolation of high oxygen affinity hemoglobins.
|
This paper describes a method for isolating high oxygen affinity hemoglobins. It involves the selective derivatisation of the cysteine residue at position 93 in the beta chain. The iodoacetamide derivative of the high oxygen affinity hemoglobin was separated from the more negatively charged iodoacetic acid derivative of HbA on DEAE-Sephadex. The method was used to isolate two high oxygen affinity hemoglobins, one of which was subsequently identified as Hb Heathrow.
|
Isolation of high oxygen affinity hemoglobins. This paper describes a method for isolating high oxygen affinity hemoglobins. It involves the selective derivatisation of the cysteine residue at position 93 in the beta chain. The iodoacetamide derivative of the high oxygen affinity hemoglobin was separated from the more negatively charged iodoacetic acid derivative of HbA on DEAE-Sephadex. The method was used to isolate two high oxygen affinity hemoglobins, one of which was subsequently identified as Hb Heathrow.
|
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] |
PMID:19380
|
The activity and distribution of gamma-glutamyl transpeptidase (y-GT) in human lung cancers serially transplanted in nude mice.
|
Gamma-glutamyl transpeptidase (y-GT) activity and distribution were investigated in different types of human lung cancers (three epidermoid carcinomas, one large cell carcinoma) which were maintained by serial transplantation in nude mice. All transplanted tumour fragments were positive for the enzyme. In the epidermoid carcinomas, y-GT levels were related to the degree of tumour differentiation. Enzyme activity in tumour fragments was always higher than that found in normal adult human lung tissue, and was, in general, maintained throughout the transplantation series.
|
The activity and distribution of gamma-glutamyl transpeptidase (y-GT) in human lung cancers serially transplanted in nude mice. Gamma-glutamyl transpeptidase (y-GT) activity and distribution were investigated in different types of human lung cancers (three epidermoid carcinomas, one large cell carcinoma) which were maintained by serial transplantation in nude mice. All transplanted tumour fragments were positive for the enzyme. In the epidermoid carcinomas, y-GT levels were related to the degree of tumour differentiation. Enzyme activity in tumour fragments was always higher than that found in normal adult human lung tissue, and was, in general, maintained throughout the transplantation series.
|
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] |
PMID:19408
|
Fortimicins A and B, new aminoglycoside antibiotics. II. Isolation, physico-chemical and chromatographic properties.
|
The aminoglycoside antibiotics fortimicins A and B produced by a naturally occurring strain Micromonospora sp. MK-70 were isolated from its fermentation beer. Fortimicins A and B were isolated as water-soluble, basic, white amorphous powders having molecular formula C17H35N5O6 and C15H32N4O5, respectively. Acid hydrolysis of fortimicin A indicated that it has one mole of glycine in its molecule while fortimicin B has not. Paper chromatography, silica-gel and carbon thin-layer chromatography revealed that fortimicins A and B are novel aminoglycoside antibiotics.
|
Fortimicins A and B, new aminoglycoside antibiotics. II. Isolation, physico-chemical and chromatographic properties. The aminoglycoside antibiotics fortimicins A and B produced by a naturally occurring strain Micromonospora sp. MK-70 were isolated from its fermentation beer. Fortimicins A and B were isolated as water-soluble, basic, white amorphous powders having molecular formula C17H35N5O6 and C15H32N4O5, respectively. Acid hydrolysis of fortimicin A indicated that it has one mole of glycine in its molecule while fortimicin B has not. Paper chromatography, silica-gel and carbon thin-layer chromatography revealed that fortimicins A and B are novel aminoglycoside antibiotics.
|
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] |
PMID:19409
|
Fortimicins A and B, new aminoglycoside antibiotics. IV. In vitro study of fortimicin A compared with other aminoglycosides.
|
The in vitro antimicrobial activity of fortimicin A, the most active member of the fortimicin complex, was compared with that of amikacin, gentamicin, sagamicin and tobramycin against 352 strains of Enterobacteriaceae and other medically significant organisms. Against most of these organisms fortimicin and amikacin had comparable levels of antimicrobial activity, generally slightly less than that of gentamicin, sagamicin or tobramycin. Fortimicin had relatively weak activity against Pseudomonas aeruginosa strains. Fortimicin shows many of the characteristics of other aminoglycoside antibiotics: (i) improved activity at alkaline pH, (ii) rapid, bactericidal action, (iii) reduced activity with increasing inoculum levels, and (iv) synergistic activity with penicillin against enterococci. The activity of fortimicin was compared to that of gentamicin, tobramycin and amikacin against a group of 95 naturally occurring, antibiotic-resistant Gram-negative bacilli other than Pseudomonas. The organisms were isolated from clinical sources and selected primarily for gentamicin resistance by the sensitivity disc test. Fortimicin showed excellent activity against this group of organisms. At a concentration of 6.2 mcg/ml, fortimicin inhibited the most strains (92.6%) followed by amikacin (90.5%), gentamicin (23.2%) and tobramycin (8.4%).
|
Fortimicins A and B, new aminoglycoside antibiotics. IV. In vitro study of fortimicin A compared with other aminoglycosides. The in vitro antimicrobial activity of fortimicin A, the most active member of the fortimicin complex, was compared with that of amikacin, gentamicin, sagamicin and tobramycin against 352 strains of Enterobacteriaceae and other medically significant organisms. Against most of these organisms fortimicin and amikacin had comparable levels of antimicrobial activity, generally slightly less than that of gentamicin, sagamicin or tobramycin. Fortimicin had relatively weak activity against Pseudomonas aeruginosa strains. Fortimicin shows many of the characteristics of other aminoglycoside antibiotics: (i) improved activity at alkaline pH, (ii) rapid, bactericidal action, (iii) reduced activity with increasing inoculum levels, and (iv) synergistic activity with penicillin against enterococci. The activity of fortimicin was compared to that of gentamicin, tobramycin and amikacin against a group of 95 naturally occurring, antibiotic-resistant Gram-negative bacilli other than Pseudomonas. The organisms were isolated from clinical sources and selected primarily for gentamicin resistance by the sensitivity disc test. Fortimicin showed excellent activity against this group of organisms. At a concentration of 6.2 mcg/ml, fortimicin inhibited the most strains (92.6%) followed by amikacin (90.5%), gentamicin (23.2%) and tobramycin (8.4%).
|
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] |
PMID:19410
|
Aminoglycoside nephrotoxicity. I. Effects of aminoglycoside antibiotics on iodohippurate accumulation in rabbit renal cortical slices.
|
The effects of aminoglycoside antibiotics on the accumulation of O-125I-hippurate (OIH) in rabbit renal cortical slices were assessed in an attempt to establish an in vitro model for aminoglycoside nephrotoxicity. Accumulation of OIH was measured after incubation of cortex slices in media containing aminoglycosides in different concentrations. All aminoglycosides depressed OIH accumulation in the following minimum concentrations: Dihydrostreptomycin and kanamycin, 2,000 microgram/ml (P less than 0.01); streptomycin and neomycin, 1,000 microgram/ml (P less than 0.05 and P less than 0.01); amikacin and tobramycin, 300 microgram/ml (P less than 0.05); gentamicin, 100 microgram/ml (P less than 0.05). A concentration of 2,000 microgram/ml caused the following reduction in OIH accumulation: Dihydrostreptomycin, 19.3%; streptomycin, 28.9%; kanamycin, 23.8%; neomycin, 62.5%; gentamicin, 68.0%; amikacin and tobramycin, 100%. Changes in pH of the incubation media after addition of aminoglycosides were only partially responsible for the observed depression of OIH accumulation and there was no evidence of substrate competition between aminoglycosides and OIH. The in vitro model described here appears to be inadequate as a sole predictor of aminoglycoside nephrotoxicity, but may provide a supplementary tool in the investigation of aminoglycoside proximal tubular cell toxicity.
|
Aminoglycoside nephrotoxicity. I. Effects of aminoglycoside antibiotics on iodohippurate accumulation in rabbit renal cortical slices. The effects of aminoglycoside antibiotics on the accumulation of O-125I-hippurate (OIH) in rabbit renal cortical slices were assessed in an attempt to establish an in vitro model for aminoglycoside nephrotoxicity. Accumulation of OIH was measured after incubation of cortex slices in media containing aminoglycosides in different concentrations. All aminoglycosides depressed OIH accumulation in the following minimum concentrations: Dihydrostreptomycin and kanamycin, 2,000 microgram/ml (P less than 0.01); streptomycin and neomycin, 1,000 microgram/ml (P less than 0.05 and P less than 0.01); amikacin and tobramycin, 300 microgram/ml (P less than 0.05); gentamicin, 100 microgram/ml (P less than 0.05). A concentration of 2,000 microgram/ml caused the following reduction in OIH accumulation: Dihydrostreptomycin, 19.3%; streptomycin, 28.9%; kanamycin, 23.8%; neomycin, 62.5%; gentamicin, 68.0%; amikacin and tobramycin, 100%. Changes in pH of the incubation media after addition of aminoglycosides were only partially responsible for the observed depression of OIH accumulation and there was no evidence of substrate competition between aminoglycosides and OIH. The in vitro model described here appears to be inadequate as a sole predictor of aminoglycoside nephrotoxicity, but may provide a supplementary tool in the investigation of aminoglycoside proximal tubular cell toxicity.
|
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] |
PMID:19413
|
Role of tissue hypermetabolism in stimulation of ventilation by dinitrophenol.
|
Several authors have hypothesized that tissue hypermetabolism accounts for increases in ventilation (VE) elicited by 2,4-dinitrophenol. However, some data in the literature indicate that stimulation of VE by isomers of dinitrophenol is unrelated to tissue metabolic rate. To test this latter concept, we compared three different isomers of dinitrophenol (i.e., 2,4-dinitrophenol (2,4-DNP), 2,5-dinitrophenol (2,5,-DNP), 2,6-dinitrophenol (2,6-DNP) with respect to stimulation of VE and with respect to stimulation of oxygen consumption (VO2). In all experiments, 3-4 mg/kg of one dinitrophenol isomer was administered to chloralose anesthetized dogs by intra-arterial infusion. 2,4-DNP elicited large increments in both VE and VO2, 2,6-DNP elicited moderate increments in both VE and VO2, whereas 2,5-DNP elicited small increments in both VE and VO2. These observations demonstrate a correlation between ventilatory and metabolic changes affected by isomers of dinitrophenol. Accordingly, these results are consistent with the hypothesis that ventilatory stimulation by congeners of dinitrophenol is related to tissue hypermetabolism.
|
Role of tissue hypermetabolism in stimulation of ventilation by dinitrophenol. Several authors have hypothesized that tissue hypermetabolism accounts for increases in ventilation (VE) elicited by 2,4-dinitrophenol. However, some data in the literature indicate that stimulation of VE by isomers of dinitrophenol is unrelated to tissue metabolic rate. To test this latter concept, we compared three different isomers of dinitrophenol (i.e., 2,4-dinitrophenol (2,4-DNP), 2,5-dinitrophenol (2,5,-DNP), 2,6-dinitrophenol (2,6-DNP) with respect to stimulation of VE and with respect to stimulation of oxygen consumption (VO2). In all experiments, 3-4 mg/kg of one dinitrophenol isomer was administered to chloralose anesthetized dogs by intra-arterial infusion. 2,4-DNP elicited large increments in both VE and VO2, 2,6-DNP elicited moderate increments in both VE and VO2, whereas 2,5-DNP elicited small increments in both VE and VO2. These observations demonstrate a correlation between ventilatory and metabolic changes affected by isomers of dinitrophenol. Accordingly, these results are consistent with the hypothesis that ventilatory stimulation by congeners of dinitrophenol is related to tissue hypermetabolism.
|
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0.014561651274561882,
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0.04886142909526825,
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0.09858877211809158,
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] |
PMID:19414
|
Column chromatographic analysis of barbiturates in their dosage forms. IV. Combinations with parabens.
|
The nature of the alkaline hydrolysis of some barbiturates in combinations with parabens (p-hydroxybenzoates) was studied with controlled variables, including temperature, viscosity, and concentrations of sodium hydroxide, barbiturate, and parabens. The kinetic studies showed that parabens could be completely hydrolyzed in strong base at 40 degrees C in 1 hr, while the barbiturate remained intact and was readily isolated by partition chromatography, Based on the theoretical results, a partition chromatographic procedure for butabarbital with parabens was devised. Standard recoveries averaged 100.7% with a standard deviation of 0.89. Kinetic data indicate that the hydrolysis of parabens could also be applied to analyze combinations with amo-, seco-, and pentobarbitals. Phenobarbital and parabens are readily separated by partition chromatographic methods without prior hydrolysis of the parabens. The low extraction constant for phenobarbital allowed its retention on a column against relatively strong solvents while the intact parabens are eluted. A slightly modified method was applied to the separation of phenobarbital from parabens. Standard recoveries average 99.9% with a standard deviation of 0.69.
|
Column chromatographic analysis of barbiturates in their dosage forms. IV. Combinations with parabens. The nature of the alkaline hydrolysis of some barbiturates in combinations with parabens (p-hydroxybenzoates) was studied with controlled variables, including temperature, viscosity, and concentrations of sodium hydroxide, barbiturate, and parabens. The kinetic studies showed that parabens could be completely hydrolyzed in strong base at 40 degrees C in 1 hr, while the barbiturate remained intact and was readily isolated by partition chromatography, Based on the theoretical results, a partition chromatographic procedure for butabarbital with parabens was devised. Standard recoveries averaged 100.7% with a standard deviation of 0.89. Kinetic data indicate that the hydrolysis of parabens could also be applied to analyze combinations with amo-, seco-, and pentobarbitals. Phenobarbital and parabens are readily separated by partition chromatographic methods without prior hydrolysis of the parabens. The low extraction constant for phenobarbital allowed its retention on a column against relatively strong solvents while the intact parabens are eluted. A slightly modified method was applied to the separation of phenobarbital from parabens. Standard recoveries average 99.9% with a standard deviation of 0.69.
|
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] |
PMID:19415
|
Application of reverse phase ion-pair partition chromatography to drugs of forensic interest.
|
A method is described for determining a wide range of abused drugs by using 1 column, a single isocratic system, and a fixed wavelength (254 nm) ultraviolet detector. Paired-ion chromatography is performed on a reverse phase muBondapak C18 column. Acidic, basic, and neutral drugs, including their corresponding salts, can be determined without prior cleanup. A counter ion, 1-heptane sulfonate, is dissolved in the aqueous organic mobile phase to give a final pH of approximately 3.5. This technique is applicable to ergot alkaloids, phenylethylamines, opium alkaloids, local anesthetics, barbiturates, and other drugs of forensic interest. Five major opium alkaloids in gum opium, namely, morphine, codeine, thebaine, narcotine, and papaverine, can be separated in approximately 20 min.
|
Application of reverse phase ion-pair partition chromatography to drugs of forensic interest. A method is described for determining a wide range of abused drugs by using 1 column, a single isocratic system, and a fixed wavelength (254 nm) ultraviolet detector. Paired-ion chromatography is performed on a reverse phase muBondapak C18 column. Acidic, basic, and neutral drugs, including their corresponding salts, can be determined without prior cleanup. A counter ion, 1-heptane sulfonate, is dissolved in the aqueous organic mobile phase to give a final pH of approximately 3.5. This technique is applicable to ergot alkaloids, phenylethylamines, opium alkaloids, local anesthetics, barbiturates, and other drugs of forensic interest. Five major opium alkaloids in gum opium, namely, morphine, codeine, thebaine, narcotine, and papaverine, can be separated in approximately 20 min.
|
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] |
PMID:19416
|
Comparison of two dioxygenases from Pseudomonas putida.
|
Catechol 2,3-dioxygenase and homoprotocatechuate 2,3-dioxygenase were purified from the same strain of Pseudomonas putida. Molecular weights and subunit sizes were similar, but amino acid compositions showed some marked differences.
|
Comparison of two dioxygenases from Pseudomonas putida. Catechol 2,3-dioxygenase and homoprotocatechuate 2,3-dioxygenase were purified from the same strain of Pseudomonas putida. Molecular weights and subunit sizes were similar, but amino acid compositions showed some marked differences.
|
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] |
PMID:19417
|
Myxospore coat synthesis in Myxococcus xanthus: enzymes associated with uridine 5'-diphosphate-N-acetylgalactosamine formation during myxospore development.
|
Activities of the enzymes glutamine synthetase (EC 6.3.1.2.), glucosamine 6-phosphate acetyltransferase (EC 2.3.1.4.), uridine 5'-diphosphate (UDP)-N-acetylglucosamine pyrophosphorylase (EC 2.7.23.), UDP-N-acetylglucosamine 4-epimerase (EC 5.1.3.7.), fructose 1,6-diphosphate phosphatase (EC 3.13.11.), L-glutamine-fructose 6-phosphate transamidase (EC 5.3.1.19.), alkaline phosphatase (EC 3.1.3.1.), and malic dehydrogenase (EC 1.1.1.37) were assayed in partially purified extracts prepared at different stages of myxospore formation and germination in liquid cultures of Myxococcus xanthus. The specific activities of the first six of these enzymes increased 4.5- to 7.5-fold after 2 h of induction with 0.5 M glycerol or 0.2 M dimethyl sulfoxide. The increase in specific activities of these six enzymes was not observed in a mutant unable to be induced with glycerol. During the first 2 to 4 h of induction and during the first hour of germination, the level of these enzymes decreased to the level characteristic of vegetative cells. It is suggested that the six enzymes are responsible for the increased conversion of fructose 1,6-diphosphate to UDP-N-acetylgalactosamine, the major precursor of the myxospore coat.
|
Myxospore coat synthesis in Myxococcus xanthus: enzymes associated with uridine 5'-diphosphate-N-acetylgalactosamine formation during myxospore development. Activities of the enzymes glutamine synthetase (EC 6.3.1.2.), glucosamine 6-phosphate acetyltransferase (EC 2.3.1.4.), uridine 5'-diphosphate (UDP)-N-acetylglucosamine pyrophosphorylase (EC 2.7.23.), UDP-N-acetylglucosamine 4-epimerase (EC 5.1.3.7.), fructose 1,6-diphosphate phosphatase (EC 3.13.11.), L-glutamine-fructose 6-phosphate transamidase (EC 5.3.1.19.), alkaline phosphatase (EC 3.1.3.1.), and malic dehydrogenase (EC 1.1.1.37) were assayed in partially purified extracts prepared at different stages of myxospore formation and germination in liquid cultures of Myxococcus xanthus. The specific activities of the first six of these enzymes increased 4.5- to 7.5-fold after 2 h of induction with 0.5 M glycerol or 0.2 M dimethyl sulfoxide. The increase in specific activities of these six enzymes was not observed in a mutant unable to be induced with glycerol. During the first 2 to 4 h of induction and during the first hour of germination, the level of these enzymes decreased to the level characteristic of vegetative cells. It is suggested that the six enzymes are responsible for the increased conversion of fructose 1,6-diphosphate to UDP-N-acetylgalactosamine, the major precursor of the myxospore coat.
|
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] |
PMID:19418
|
Induction of the acetamidase of Aspergillus nidulans by acetate metabolism.
|
Growth tests and enzyme determinations strongly suggest that the acetamidase of Aspergillus nidulans is induced by a product of acetate metabolism rather than the substrate, acetamide. The cis-dominant mutation, amdI9, which is closely linked to amdS, the structural gene for the acetamidase, results in greatly increased sensitivity to induction by acetate metabolism. Propionate, L-threonine, and ethanol also result in acetamidase induction. Mutations in the facA, facB, and facC genes, which lead to low levels of acetyl-coenzyme A synthase, are epistatic to the amdI9 mutation for strong growth on acetamide medium and abolish acetamide and propionamide induction of the acetamidase and isocitrate lyase enzymes. Acetate, L-threonine, and ethanol, however, can induce these enzymes in strains containing facA and facC lesions but not in strains containing a facB lesion. The evidence suggests that acetamidase and isocitrate lyase may be induced by a similar mechanism.
|
Induction of the acetamidase of Aspergillus nidulans by acetate metabolism. Growth tests and enzyme determinations strongly suggest that the acetamidase of Aspergillus nidulans is induced by a product of acetate metabolism rather than the substrate, acetamide. The cis-dominant mutation, amdI9, which is closely linked to amdS, the structural gene for the acetamidase, results in greatly increased sensitivity to induction by acetate metabolism. Propionate, L-threonine, and ethanol also result in acetamidase induction. Mutations in the facA, facB, and facC genes, which lead to low levels of acetyl-coenzyme A synthase, are epistatic to the amdI9 mutation for strong growth on acetamide medium and abolish acetamide and propionamide induction of the acetamidase and isocitrate lyase enzymes. Acetate, L-threonine, and ethanol, however, can induce these enzymes in strains containing facA and facC lesions but not in strains containing a facB lesion. The evidence suggests that acetamidase and isocitrate lyase may be induced by a similar mechanism.
|
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] |
PMID:19419
|
Sodium ion-stimulated alpha-[1-14C]aminoisobutyric acid uptake in alkalophilic Bacillus species.
|
Alkalophilic Bacillus no. 8-1 grows well in alkaline media containing 2.5 to 5% NaCl. The uptake of alpha-aminoisobutyric acid (AIB) into the cells is stimulated by the addition of NaCl (Na+) up to a concentration of 0.2 M, but other monovalent cations such as K+, Li+, or NH4+ cannot substitute for Na+. The kinetic studies reveal that, when the Na+ concentration increases from 0.02 to 0.2 M in alkaline medium, the Km for transport decreases, whereas Vmax remains almost constant. Competition studies indicate that glycine, L-alanine, L-serine, and AIB share common carriers for the transport of the compounds into cells. Other alkalophilic bacteria are also found to require Na+ for the uptake of AIB into the cells.
|
Sodium ion-stimulated alpha-[1-14C]aminoisobutyric acid uptake in alkalophilic Bacillus species. Alkalophilic Bacillus no. 8-1 grows well in alkaline media containing 2.5 to 5% NaCl. The uptake of alpha-aminoisobutyric acid (AIB) into the cells is stimulated by the addition of NaCl (Na+) up to a concentration of 0.2 M, but other monovalent cations such as K+, Li+, or NH4+ cannot substitute for Na+. The kinetic studies reveal that, when the Na+ concentration increases from 0.02 to 0.2 M in alkaline medium, the Km for transport decreases, whereas Vmax remains almost constant. Competition studies indicate that glycine, L-alanine, L-serine, and AIB share common carriers for the transport of the compounds into cells. Other alkalophilic bacteria are also found to require Na+ for the uptake of AIB into the cells.
|
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-0.04658741503953934,
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0.0439135767519474,
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-0.006620973348617554,
0.07328713685274124,
0.05544635280966759
] |
PMID:19420
|
Metabolism of 6-aminonicotinic acid in Escherichia coli.
|
A late-log-phase culture of an Escherichia coli nadB pncA double mutant took up 6-[7-14C]aminonicotinic acid and excreted 6-[14C]aminonicotinamide. This mutant also accumulated intracellularly several radioactive compounds which have been tentatively identified as 6-amino analogs of compounds in the pyridine nucleotide cycle. It is concluded that 6-aminonicotinamide and 6-aminonicotinic acid probably exert at least a portion of their bacteriostatic effects by being metabolized, by the enzymes of the pyridine nucleotide cycle, to 6-aminonicotinamide adenine dinucleotide and 6-aminonicotinamide adenine dinucleotide phosphate. These compounds are not electron acceptors and are known inhibitors of some pyridine nucleotide-linked dehydrogenases.
|
Metabolism of 6-aminonicotinic acid in Escherichia coli. A late-log-phase culture of an Escherichia coli nadB pncA double mutant took up 6-[7-14C]aminonicotinic acid and excreted 6-[14C]aminonicotinamide. This mutant also accumulated intracellularly several radioactive compounds which have been tentatively identified as 6-amino analogs of compounds in the pyridine nucleotide cycle. It is concluded that 6-aminonicotinamide and 6-aminonicotinic acid probably exert at least a portion of their bacteriostatic effects by being metabolized, by the enzymes of the pyridine nucleotide cycle, to 6-aminonicotinamide adenine dinucleotide and 6-aminonicotinamide adenine dinucleotide phosphate. These compounds are not electron acceptors and are known inhibitors of some pyridine nucleotide-linked dehydrogenases.
|
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] |
PMID:19421
|
Allantoin transport in Saccharomyces cerevisiae.
|
Allantoin uptake in both growing and resting cultures of Saccharomyces cerevisiae occurs by a low-Km (ca. 15 micrometer) transport system that uses energy that is likely generated in the cytoplasm. This conclusion was based on the observation that transport did not occur in the absence of glucose or the presence of dinitrophenol, carbonyl cyanide-m-chloro-phenyl hydrazine, fluoride, or arsenate ions. Normal uptake was observed, however, in the presence of cyanide. The rate of accumulation was maximal at pH 5.2. In contrast to the urea transport system, allantoin uptake appeared to be unidirectional. Preloaded, radioactive allantoin was not lost from cells suspended in allantoin-free buffer and did not exchange with exogenously added, nonradioactive allantoin. Treatment of preloaded cells with nystatin, however, released the accumulated radioactivity. Allantoin accumulated within cells was isolated and shown to be chemically unaltered.
|
Allantoin transport in Saccharomyces cerevisiae. Allantoin uptake in both growing and resting cultures of Saccharomyces cerevisiae occurs by a low-Km (ca. 15 micrometer) transport system that uses energy that is likely generated in the cytoplasm. This conclusion was based on the observation that transport did not occur in the absence of glucose or the presence of dinitrophenol, carbonyl cyanide-m-chloro-phenyl hydrazine, fluoride, or arsenate ions. Normal uptake was observed, however, in the presence of cyanide. The rate of accumulation was maximal at pH 5.2. In contrast to the urea transport system, allantoin uptake appeared to be unidirectional. Preloaded, radioactive allantoin was not lost from cells suspended in allantoin-free buffer and did not exchange with exogenously added, nonradioactive allantoin. Treatment of preloaded cells with nystatin, however, released the accumulated radioactivity. Allantoin accumulated within cells was isolated and shown to be chemically unaltered.
|
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] |
PMID:19422
|
Cyclic adenosine 3',5'-monophosphate regulation of membrane energetics in Escherichia coli.
|
Mutants of Escherichia coli K-12 lacking functional adenylate cyclase (cya) or the cyclic adenosine 3',5'-monophosphate (cAMP) receptor protein (crp) were compared with their wild type to evaluate the role played by the cAMP-cAMP receptor protein complex in regulating this organism's membrane-associated bioenergetic functions. Both mutants were found to be equally defective in carrying out various electron transport activities. In particular, their capacity for synthesizing a functional oxygen-linked transhydrogenase system was totally repressed, and their content of flavin adenine dinucleotide was reduced by approximately 85%. In addition, it was found that the mutant strains had a decreased ability to generate a protonmotive force and to use this chemiosmotic force to generate adenosine 5'-triphosphate. All these membrane-associated dysfunctions were completely restored to the wild-type state when the cya cells were grown in the presence of exogenous cAMP. As would be expected if these controls were operating at the transcriptional level, the crp cells retained the mutant character even when grown in the presence of this cyclic nucleotide.
|
Cyclic adenosine 3',5'-monophosphate regulation of membrane energetics in Escherichia coli. Mutants of Escherichia coli K-12 lacking functional adenylate cyclase (cya) or the cyclic adenosine 3',5'-monophosphate (cAMP) receptor protein (crp) were compared with their wild type to evaluate the role played by the cAMP-cAMP receptor protein complex in regulating this organism's membrane-associated bioenergetic functions. Both mutants were found to be equally defective in carrying out various electron transport activities. In particular, their capacity for synthesizing a functional oxygen-linked transhydrogenase system was totally repressed, and their content of flavin adenine dinucleotide was reduced by approximately 85%. In addition, it was found that the mutant strains had a decreased ability to generate a protonmotive force and to use this chemiosmotic force to generate adenosine 5'-triphosphate. All these membrane-associated dysfunctions were completely restored to the wild-type state when the cya cells were grown in the presence of exogenous cAMP. As would be expected if these controls were operating at the transcriptional level, the crp cells retained the mutant character even when grown in the presence of this cyclic nucleotide.
|
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] |
PMID:19423
|
Regulation of the Neurospora crassa assimilatory nitrate reductase.
|
Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-nitrate reductase from Neurospora crassa was purified and found to be stimulated by certain amino acids, citrate, and ethylenediaminetetraacetic acid (EDTA). Stimulation by citrate and the amino acids was dependent upon the prior removal of EDTA from the enzyme preparations, since low quantities of EDTA resulted in maximal stimulation. Removal of EDTA from enzyme preparations by dialysis against Chelex-containing buffer resulted in a loss of nitrate reductase activity. Addition of alanine, arginine, glycine, glutamine, glutamate, histidine, tryptophan, and citrate restored and stimulated nitrate reductase activity from 29- to 46-fold. The amino acids tested altered the Km of NADPH-nitrate reductase for NADPH but did not significantly change that for nitrate. The Km of nitrate reductase for NADPH increased with increasing concentrations of histidine but decreased with increasing concentrations of glutamine. Amino acid modulation of NADPH-nitrate reductase activity is discussed in relation to the conservation of energy (NADPH) by Neurospora when nitrate is the nitrogen source.
|
Regulation of the Neurospora crassa assimilatory nitrate reductase. Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-nitrate reductase from Neurospora crassa was purified and found to be stimulated by certain amino acids, citrate, and ethylenediaminetetraacetic acid (EDTA). Stimulation by citrate and the amino acids was dependent upon the prior removal of EDTA from the enzyme preparations, since low quantities of EDTA resulted in maximal stimulation. Removal of EDTA from enzyme preparations by dialysis against Chelex-containing buffer resulted in a loss of nitrate reductase activity. Addition of alanine, arginine, glycine, glutamine, glutamate, histidine, tryptophan, and citrate restored and stimulated nitrate reductase activity from 29- to 46-fold. The amino acids tested altered the Km of NADPH-nitrate reductase for NADPH but did not significantly change that for nitrate. The Km of nitrate reductase for NADPH increased with increasing concentrations of histidine but decreased with increasing concentrations of glutamine. Amino acid modulation of NADPH-nitrate reductase activity is discussed in relation to the conservation of energy (NADPH) by Neurospora when nitrate is the nitrogen source.
|
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] |
PMID:19424
|
Alteration of the Bacillus subtilis glutamine synthetase results in overproduction of the enzyme.
|
A mutational leading to glutamine auxotrophy was located near a 5-fluorouracil resistance marker in the citB-thyA region of the Bacillus subtilis chromosome. This mutation resulted in a glutamine synthetase with altered kinetic and feedback properties. The specific activity of manganese-stimulated glutamine synthetase activity in crude extracts was 18-fold higher, and the magnesium-stimulated activity was about 30% that of the wild type. Quantitation of the enzyme by precipitation with antibody prepared against pure enzyme confirmed the presence of high enzyme levels in the mutant. This mutation is very closely linked (recombination index of 0.03) to another glutamine auxotroph containing enzyme with altered electrophoretic and heat sensitivity properties. Mutations in the structural gene for glutamine synthetase may result not only in altered catalytic and regulatory properties but also in altered production of the enzyme.
|
Alteration of the Bacillus subtilis glutamine synthetase results in overproduction of the enzyme. A mutational leading to glutamine auxotrophy was located near a 5-fluorouracil resistance marker in the citB-thyA region of the Bacillus subtilis chromosome. This mutation resulted in a glutamine synthetase with altered kinetic and feedback properties. The specific activity of manganese-stimulated glutamine synthetase activity in crude extracts was 18-fold higher, and the magnesium-stimulated activity was about 30% that of the wild type. Quantitation of the enzyme by precipitation with antibody prepared against pure enzyme confirmed the presence of high enzyme levels in the mutant. This mutation is very closely linked (recombination index of 0.03) to another glutamine auxotroph containing enzyme with altered electrophoretic and heat sensitivity properties. Mutations in the structural gene for glutamine synthetase may result not only in altered catalytic and regulatory properties but also in altered production of the enzyme.
|
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] |
PMID:19425
|
Partial purification and characterization of L-lactate dehydrogenase isozymes from sweet potato roots.
|
Lactate dehydrogenase [L-lactate: NAD oxidoreductase, EC 1.1.1.27] was isolated from sweet potato root tissues. Two species of the enzyme (isozymes I and II) were separated by DE-52 cellulose column chromatography from healthy, cut, and black-rot diseased tissues. Isozymes I and II were purified from healthy and diseased tissues, respectively. Reduction of pyruvate by NADH with either isozyme I or II was inhibited by pyruvate at high concentrations, by NAD+ and by several mononucleotides. Isozyme I was inhibited by a lower concentration of adenine nucleotide than isozyme II, and Km for pyruvate was increased markedly at acidic pH in the case of isozyme I, but only slightly in the case of isozyme II. The molecular weights of both isozymes were determined to be 150,000 and they were found to be charge isomers by polyacrylamide gel electrophoresis. The enzyme activity increased in response to infection by black-rot fungus but decreased in response to cutting.
|
Partial purification and characterization of L-lactate dehydrogenase isozymes from sweet potato roots. Lactate dehydrogenase [L-lactate: NAD oxidoreductase, EC 1.1.1.27] was isolated from sweet potato root tissues. Two species of the enzyme (isozymes I and II) were separated by DE-52 cellulose column chromatography from healthy, cut, and black-rot diseased tissues. Isozymes I and II were purified from healthy and diseased tissues, respectively. Reduction of pyruvate by NADH with either isozyme I or II was inhibited by pyruvate at high concentrations, by NAD+ and by several mononucleotides. Isozyme I was inhibited by a lower concentration of adenine nucleotide than isozyme II, and Km for pyruvate was increased markedly at acidic pH in the case of isozyme I, but only slightly in the case of isozyme II. The molecular weights of both isozymes were determined to be 150,000 and they were found to be charge isomers by polyacrylamide gel electrophoresis. The enzyme activity increased in response to infection by black-rot fungus but decreased in response to cutting.
|
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] |
PMID:19426
|
Studies on sterol-ester hydrolase from Fusarium oxysporum. I. Partial purification and properties.
|
1. A search for a long chain fatty acyl sterol-ester hydrolase in microorganisms led to the isolation from soil of five strains belonging to Fusarium sp. which produced strong activity in the culture medium. 2. The cholesterol esterase from Fusarium oxysporum IGH-2 was purified about 270-fold by means of CaCl2 precipitation and Sephadex G-75 column chromatography. 3. The cholesterol esterase was activated by adekatol and Triton X-100. It was inhibited by lecithin and lysolecithin, and completely inactivated by heat treatment (60 degrees C for 30 min, at pH 7.0). 4. The optimum pH of the enzyme was found to be around 7.0. 5. Among various cholesterol esters tested, cholesterol linoleate was the most suitable substrate. 6. Cholesterol esters in serum were also hydrolyzed by this enzyme.
|
Studies on sterol-ester hydrolase from Fusarium oxysporum. I. Partial purification and properties. 1. A search for a long chain fatty acyl sterol-ester hydrolase in microorganisms led to the isolation from soil of five strains belonging to Fusarium sp. which produced strong activity in the culture medium. 2. The cholesterol esterase from Fusarium oxysporum IGH-2 was purified about 270-fold by means of CaCl2 precipitation and Sephadex G-75 column chromatography. 3. The cholesterol esterase was activated by adekatol and Triton X-100. It was inhibited by lecithin and lysolecithin, and completely inactivated by heat treatment (60 degrees C for 30 min, at pH 7.0). 4. The optimum pH of the enzyme was found to be around 7.0. 5. Among various cholesterol esters tested, cholesterol linoleate was the most suitable substrate. 6. Cholesterol esters in serum were also hydrolyzed by this enzyme.
|
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] |
PMID:19427
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Isolation and partial characterization of the serum low density lipoprotein from bullfrog, Rana catesbeiana.
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The chemical and physical properties of bullfrog serum low density lipoprotein (LDL) were investigated. On a weight percentage basis, LDL contained cholesterol ester, 30.3%; cholesterol, 5.6%; triglyceride, 12.5%; phospholipids, 23.3%; and protein, 22.4%. The fatty acid compositions of triglycerides and major phospholipids from the bullfrog serum LDL were quite similar to those of human serum LDL. However, the fatty acid composition of the chlesterol ester from the bullfrog serum LDL was quite different from that of the human serum LDL. The average particle weight, determined by gel filtration, was 2 X 10(6) daltons. This value is very close to that of human LDL. In the fluorescence emission spectrum of bullfrog serum LDL, the emission maximum was 324 nm. The amino acid composition of the apo-LDL resembled that of human apo-LDL.
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Isolation and partial characterization of the serum low density lipoprotein from bullfrog, Rana catesbeiana. The chemical and physical properties of bullfrog serum low density lipoprotein (LDL) were investigated. On a weight percentage basis, LDL contained cholesterol ester, 30.3%; cholesterol, 5.6%; triglyceride, 12.5%; phospholipids, 23.3%; and protein, 22.4%. The fatty acid compositions of triglycerides and major phospholipids from the bullfrog serum LDL were quite similar to those of human serum LDL. However, the fatty acid composition of the chlesterol ester from the bullfrog serum LDL was quite different from that of the human serum LDL. The average particle weight, determined by gel filtration, was 2 X 10(6) daltons. This value is very close to that of human LDL. In the fluorescence emission spectrum of bullfrog serum LDL, the emission maximum was 324 nm. The amino acid composition of the apo-LDL resembled that of human apo-LDL.
|
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] |
PMID:19428
|
Separation of newly-synthesized RNA by organomercurial agarose affinity chromatography.
|
Mouse myeloma cells, MOPC-31C, were incubated in the presence of 2-thiouridine and newly-synthesized RNA which appeared to contain 2-thioUMP as a constituent was separated from preexisting RNA by affinity chromatography using organomercurial agarose as a support. Both pH and salt concentration greatly affected the specific adsorption of the newly-synthesized RNA on the column. Under optimal conditions the rate of adsorption of the newly-synthesized RNA on the column was proportional to the logarithmic concentration of 2-thiouridine in the culture medium. Furthermore, at a given concentration of 2-thiouridine in the medium, a shorter incubation period caused a reduction of the rate of RNA adsorption on the column. The molecular size distributions of both total RNA and the adsorbed fraction, synthesized during 30 min in the presence of 2-thiouridine, were similar to that of RNA synthesized in the absence of the drug.
|
Separation of newly-synthesized RNA by organomercurial agarose affinity chromatography. Mouse myeloma cells, MOPC-31C, were incubated in the presence of 2-thiouridine and newly-synthesized RNA which appeared to contain 2-thioUMP as a constituent was separated from preexisting RNA by affinity chromatography using organomercurial agarose as a support. Both pH and salt concentration greatly affected the specific adsorption of the newly-synthesized RNA on the column. Under optimal conditions the rate of adsorption of the newly-synthesized RNA on the column was proportional to the logarithmic concentration of 2-thiouridine in the culture medium. Furthermore, at a given concentration of 2-thiouridine in the medium, a shorter incubation period caused a reduction of the rate of RNA adsorption on the column. The molecular size distributions of both total RNA and the adsorbed fraction, synthesized during 30 min in the presence of 2-thiouridine, were similar to that of RNA synthesized in the absence of the drug.
|
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] |
PMID:19429
|
Interaction of Asp. melleus Semi-alkaline protease with benzeneboronic acid.
|
Benzeneboronic acid (BBA), a possible transition-state analog for serine proteases, was found to inhibit Asp. melleus semi-alkaline protease [EC 3.4.21.15]. The pH dependence of inhibitor constants was studied by the pH-stat method using N-acetyl-L-tyrosine ethyl ester as a substrate at 25 degrees C. From the pH dependence of the association constant (reciprocal inhibitor constant), a pK value of 6.6, which may be attributable to the catalytic histidine residue of the enzyme, was estimated. The BBA-enzyme interaction was studied kinetically by the temperature-jump method. Apparent association and dissociation rate constants were determined at pH 6.5.
|
Interaction of Asp. melleus Semi-alkaline protease with benzeneboronic acid. Benzeneboronic acid (BBA), a possible transition-state analog for serine proteases, was found to inhibit Asp. melleus semi-alkaline protease [EC 3.4.21.15]. The pH dependence of inhibitor constants was studied by the pH-stat method using N-acetyl-L-tyrosine ethyl ester as a substrate at 25 degrees C. From the pH dependence of the association constant (reciprocal inhibitor constant), a pK value of 6.6, which may be attributable to the catalytic histidine residue of the enzyme, was estimated. The BBA-enzyme interaction was studied kinetically by the temperature-jump method. Apparent association and dissociation rate constants were determined at pH 6.5.
|
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] |
PMID:19430
|
Thermal denaturation of cytochromes c of horse cow, and Candida krusei in aqueous guanidine hydrochloride.
|
Thermal denaturation of cytochromes c of horse, cow, and Candida krusei in aqueous guanidine hydrochloride in the neutral pH region was studied by means of absorption and optical rotation measurements. The values of standard free energy change upon denaturation were estimated over the temperature range from 3 to 51 degrees C. Large differences in the heat capacity of the native and denatured states amounting to several kcal/mol-deg were obtained for all three kinds of cytochromes c. These lead to a change in the sign of both the enthalpy and entropy change of denaturation, with maximum stability of the native state at 12 degrees C for horse and bovine cytochromes c and at 9 degrees C for Candida krusei.
|
Thermal denaturation of cytochromes c of horse cow, and Candida krusei in aqueous guanidine hydrochloride. Thermal denaturation of cytochromes c of horse, cow, and Candida krusei in aqueous guanidine hydrochloride in the neutral pH region was studied by means of absorption and optical rotation measurements. The values of standard free energy change upon denaturation were estimated over the temperature range from 3 to 51 degrees C. Large differences in the heat capacity of the native and denatured states amounting to several kcal/mol-deg were obtained for all three kinds of cytochromes c. These lead to a change in the sign of both the enthalpy and entropy change of denaturation, with maximum stability of the native state at 12 degrees C for horse and bovine cytochromes c and at 9 degrees C for Candida krusei.
|
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] |
PMID:19431
|
Dihydrodipicolinate reductases from Bacillus cereus and Bacillus megaterium.
|
Dyhydrodipicolinate reductases were purified 100-fold from crude extracts of B. cereus and B. megaterium and their properties were compared with those of the reductase from B. subtilis. The molecular weights of the reductases of B. cereus and B. megaterium were fount to be 155,000 and 150,000, respectively. These reductases were shown to be free of flavin, unlike the B. subtilis enzyme, which contains flavin. Both NADPH and NADH acted as coenzymes for these two reductases. NADPH being three or four times more effective than NADH. The Km values for NADPH and dihydrodipicolinate were 8 micrometer and 62 micrometer, respectively, with B. cereus reductase, and 13 micrometer and 59 micrometer with B. megaterium reductase. The pH optima of the enzymes from B. cereus and B. megaterium were pH 7.4 and 7.2, respectively. The reductases were inhibited by dipicolinate noncompetitively with respect to dihydrodipicolinate and the Ki values were 85 micrometer and 140 micrometer, respectively. Lysine and diaminopimelate were not inhibitory. The properties of the reductases from B. cereus and B. megaterium were similar, but they differed considerably from those of the B. subtilis enzyme. However, all three Bacillus reductases were markedly inhibited by dipicolinate, unlike the enzyme from E. coli.
|
Dihydrodipicolinate reductases from Bacillus cereus and Bacillus megaterium. Dyhydrodipicolinate reductases were purified 100-fold from crude extracts of B. cereus and B. megaterium and their properties were compared with those of the reductase from B. subtilis. The molecular weights of the reductases of B. cereus and B. megaterium were fount to be 155,000 and 150,000, respectively. These reductases were shown to be free of flavin, unlike the B. subtilis enzyme, which contains flavin. Both NADPH and NADH acted as coenzymes for these two reductases. NADPH being three or four times more effective than NADH. The Km values for NADPH and dihydrodipicolinate were 8 micrometer and 62 micrometer, respectively, with B. cereus reductase, and 13 micrometer and 59 micrometer with B. megaterium reductase. The pH optima of the enzymes from B. cereus and B. megaterium were pH 7.4 and 7.2, respectively. The reductases were inhibited by dipicolinate noncompetitively with respect to dihydrodipicolinate and the Ki values were 85 micrometer and 140 micrometer, respectively. Lysine and diaminopimelate were not inhibitory. The properties of the reductases from B. cereus and B. megaterium were similar, but they differed considerably from those of the B. subtilis enzyme. However, all three Bacillus reductases were markedly inhibited by dipicolinate, unlike the enzyme from E. coli.
|
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] |
PMID:19432
|
Two omega-amino acid transaminases from Bacillus cereus.
|
Bacillus cereus strain K-22 produced two distinct omega-amino acid transaminases, one catalyzing the transamination between beta-alanine and pyruvic acid and the other that between gamma-aminobutyric acid and alpha-ketoglutaric aic. The two enzymes were partially purified and separated from each other by various chromatographies. beta-Alanine:pyruvic acid transaminase and gamma-aminobutyric acid:alpha-ketoglutaric acid transaminase were induced by the addition of beta-alanine and gamma-aminobutyric acid, respectively, to the growth medium. beta-Alanine transaminase showed an optimum pH of 10.0 and optimum temperature of 35 degrees C, and its Km values for beta-alanine and pyruvic acid were both 1.1 mM. gamma-Aminobutyric acid, epsilon-aminocaproic acid, 2-aminoethylphosphonic acid, and propylamine showed about 30-40% of the activity of beta-alanine as amino donors, and oxalacetic acid was as good an amino acceptor as pyruvic acid. The optimum pH and temperature of gamma-aminobutyric acid transaminase were 9.0 and 50 degrees C, respectively, and its Km value for gamma-aminobutyric acid was 2.8 mM, while that for alpha-ketoglutaric acid was 2.3 mM. gamma-Aminobutyric acid and delta-aminovaleric acid were good amino donors but other omega-amino acids were virtually inactive with gamma-aminobutyric acid transaminase; alpha-ketoglutaric acid, and to a lesser extent glyoxylic acid, were active amino acceptors. Sulfhydryl reagents specifically activated gamma-aminobutyric acid transaminase.
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Two omega-amino acid transaminases from Bacillus cereus. Bacillus cereus strain K-22 produced two distinct omega-amino acid transaminases, one catalyzing the transamination between beta-alanine and pyruvic acid and the other that between gamma-aminobutyric acid and alpha-ketoglutaric aic. The two enzymes were partially purified and separated from each other by various chromatographies. beta-Alanine:pyruvic acid transaminase and gamma-aminobutyric acid:alpha-ketoglutaric acid transaminase were induced by the addition of beta-alanine and gamma-aminobutyric acid, respectively, to the growth medium. beta-Alanine transaminase showed an optimum pH of 10.0 and optimum temperature of 35 degrees C, and its Km values for beta-alanine and pyruvic acid were both 1.1 mM. gamma-Aminobutyric acid, epsilon-aminocaproic acid, 2-aminoethylphosphonic acid, and propylamine showed about 30-40% of the activity of beta-alanine as amino donors, and oxalacetic acid was as good an amino acceptor as pyruvic acid. The optimum pH and temperature of gamma-aminobutyric acid transaminase were 9.0 and 50 degrees C, respectively, and its Km value for gamma-aminobutyric acid was 2.8 mM, while that for alpha-ketoglutaric acid was 2.3 mM. gamma-Aminobutyric acid and delta-aminovaleric acid were good amino donors but other omega-amino acids were virtually inactive with gamma-aminobutyric acid transaminase; alpha-ketoglutaric acid, and to a lesser extent glyoxylic acid, were active amino acceptors. Sulfhydryl reagents specifically activated gamma-aminobutyric acid transaminase.
|
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] |
PMID:19433
|
Affinity labeling of adenine nucleotide-related enzymes with reactive adenine nucleotide analogs. II. Affinity labeling of phosphoglycerate kinase with a reactive AMP analog.
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Affinity labeling of yeast and B. stearothermophilus phosphoglycerate kinases with a reactive AMP analog, N6-(p-bromoacetaminobenzyl)-AMP was examined. Complete loss of enzyme activity was observed when 1 mol of the reagent had reacted per mol of either enzyme. Results on the effect of pH and substrate addition on the inactivation, titration of SH groups before and after modification, and kinetic studies with AMP analogs suggest that the modification occurs at one amino group at or near the substrate binding site. General affinity labeling of kinases is discussed based on the results obtained.
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Affinity labeling of adenine nucleotide-related enzymes with reactive adenine nucleotide analogs. II. Affinity labeling of phosphoglycerate kinase with a reactive AMP analog. Affinity labeling of yeast and B. stearothermophilus phosphoglycerate kinases with a reactive AMP analog, N6-(p-bromoacetaminobenzyl)-AMP was examined. Complete loss of enzyme activity was observed when 1 mol of the reagent had reacted per mol of either enzyme. Results on the effect of pH and substrate addition on the inactivation, titration of SH groups before and after modification, and kinetic studies with AMP analogs suggest that the modification occurs at one amino group at or near the substrate binding site. General affinity labeling of kinases is discussed based on the results obtained.
|
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] |
PMID:19435
|
Effect of halide anions on the binding of FAD to D-amino acid oxidase and the tryptophanyl fluorescence of the apoenzyme.
|
The quenching of tryptophanyl fluorescence of native and denatured D-amino acid oxidase from hog kidney was measured. About 60% of the tryptophanyl fluorescence of the native apoenzyme was quenched by iodide at pH 8.3, and 25 degrees C. All of the tryptophanyl fluorescence of the apoenzyme in 6 M guanidine hydrochloride was quenched. The tryptophanyl fluorescence quenching of the holoenzyme by 1-methyl nicotinamide chloride was low in comparison with that of the apoenzyme. These results of the quenching experiments are discussed based on the intermolecular collision quenching mechanism. By measuring the fluorescence intensities of the tryptophanyl residues and FAD of the holoenzyme solution, and the fluorescence polarization of the holoenzyme solution containing halide anions such as iodide, bromide, chloride, or fluoride, we found that FAD dissociates from the holoenzyme in the presence of iodide, bromide, or chloride, and the ability to dissociate FAD from the holoenzyme decreases in order iodide, bromide, and chloride. However, fluoride seems to enhance the association reaction of FAD with the apoenzyme. These results were consistent with the visible absorption spectra and derivative spectra of free FAD and the holoenzyme in the presence and absence of halide anions.
|
Effect of halide anions on the binding of FAD to D-amino acid oxidase and the tryptophanyl fluorescence of the apoenzyme. The quenching of tryptophanyl fluorescence of native and denatured D-amino acid oxidase from hog kidney was measured. About 60% of the tryptophanyl fluorescence of the native apoenzyme was quenched by iodide at pH 8.3, and 25 degrees C. All of the tryptophanyl fluorescence of the apoenzyme in 6 M guanidine hydrochloride was quenched. The tryptophanyl fluorescence quenching of the holoenzyme by 1-methyl nicotinamide chloride was low in comparison with that of the apoenzyme. These results of the quenching experiments are discussed based on the intermolecular collision quenching mechanism. By measuring the fluorescence intensities of the tryptophanyl residues and FAD of the holoenzyme solution, and the fluorescence polarization of the holoenzyme solution containing halide anions such as iodide, bromide, chloride, or fluoride, we found that FAD dissociates from the holoenzyme in the presence of iodide, bromide, or chloride, and the ability to dissociate FAD from the holoenzyme decreases in order iodide, bromide, and chloride. However, fluoride seems to enhance the association reaction of FAD with the apoenzyme. These results were consistent with the visible absorption spectra and derivative spectra of free FAD and the holoenzyme in the presence and absence of halide anions.
|
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] |
PMID:19437
|
Purification and some properties of rabbit stomach myosin.
|
Myosin from rabbit stomach was highly purified by ammonium sulfate fractionation in the presence of ATP and MgCl2, ultracentrifugation and Sepharose 4B chromatography. The myosin composed of one heavy and two light chains as determined by SDS-gel electrophoresis. The molecular weights of the light chains were the same as those of gizzard myosin, about 20,000 and 17,000, respectively. The pH-activity curve and the KCl concentration dependency of Ca-ATPase of the stomach myosin were similar to those of other smooth muscle myosins. The stomach myosin was more resistant to pepsin digestion than skeletal myosin. Other proteolytic enzymes, trypsin, chymotrypsin, papain, and nagarse, digested the myosin in the same way as skeletal myosin.
|
Purification and some properties of rabbit stomach myosin. Myosin from rabbit stomach was highly purified by ammonium sulfate fractionation in the presence of ATP and MgCl2, ultracentrifugation and Sepharose 4B chromatography. The myosin composed of one heavy and two light chains as determined by SDS-gel electrophoresis. The molecular weights of the light chains were the same as those of gizzard myosin, about 20,000 and 17,000, respectively. The pH-activity curve and the KCl concentration dependency of Ca-ATPase of the stomach myosin were similar to those of other smooth muscle myosins. The stomach myosin was more resistant to pepsin digestion than skeletal myosin. Other proteolytic enzymes, trypsin, chymotrypsin, papain, and nagarse, digested the myosin in the same way as skeletal myosin.
|
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] |
PMID:19438
|
Accumulation of phosphoenolpyruvate in red cells incubated with the phosphate ester in an acidified isotonic sucrose medium.
|
Accumulation of exogenous phosphoenolpyruvate against the concentration gradient was observed when human red cells were incubated in an acidified isotonic sucrose medium. Fluoride increased the apparent accumulation by inhibition of the intracellular metabolic interconversion of the phosphate compound. The accumulation appeared to be specific for phosphoenolpyruvate and the accumulation rate for 3-phosphoglycerate, which has a molecular size and pKa similar to those of phosphoenolpyruvate, was less than one-tenth of the rate of phosphoenolpyruvate. Red cells incubated in the acidified sucrose medium tended to adhere to each other when examined with a scanning electron microscope.
|
Accumulation of phosphoenolpyruvate in red cells incubated with the phosphate ester in an acidified isotonic sucrose medium. Accumulation of exogenous phosphoenolpyruvate against the concentration gradient was observed when human red cells were incubated in an acidified isotonic sucrose medium. Fluoride increased the apparent accumulation by inhibition of the intracellular metabolic interconversion of the phosphate compound. The accumulation appeared to be specific for phosphoenolpyruvate and the accumulation rate for 3-phosphoglycerate, which has a molecular size and pKa similar to those of phosphoenolpyruvate, was less than one-tenth of the rate of phosphoenolpyruvate. Red cells incubated in the acidified sucrose medium tended to adhere to each other when examined with a scanning electron microscope.
|
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] |
PMID:19439
|
A sensitive substrate for the clotting enzyme in horseshoe crab hemocytes.
|
An endotoxin-activated hemocyte lysate from horseshoe crab (Tachypleus and Limulus) was found to hydrolyze specifically BZ-Ile-Glu-Gly-Arg-p-nitroanilide, which was recently introduced as the substrate for assay of the blood coagulation factor, Factor Xa. Further, this amidase activity increased by increasing the concentration of bacterial endotoxin (Salmonella minnesota R595) added to the lysate. Thus, the measurement of the amidase activity in the hemocyte lysate can be very useful to detect and determine the endotoxin.
|
A sensitive substrate for the clotting enzyme in horseshoe crab hemocytes. An endotoxin-activated hemocyte lysate from horseshoe crab (Tachypleus and Limulus) was found to hydrolyze specifically BZ-Ile-Glu-Gly-Arg-p-nitroanilide, which was recently introduced as the substrate for assay of the blood coagulation factor, Factor Xa. Further, this amidase activity increased by increasing the concentration of bacterial endotoxin (Salmonella minnesota R595) added to the lysate. Thus, the measurement of the amidase activity in the hemocyte lysate can be very useful to detect and determine the endotoxin.
|
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] |
PMID:19440
|
Biosynthesis of glycogen in Neurospora crassa. Existence of a glucoproteic intermediate in the initiation process.
|
A soluble enzyme preparation (20,000 X g supernatant fraction), prepared from the mycelia of wild-type Neurospora crassa, was capable of transferring [14C]glucose from UDP-[14C]glucose into both trichloroacetic acid (TCA)-soluble and TCA-insoluble macromolecule products in the absence of added primer. These reactions did not require either high concentrations of salts or any other chemical reagents. Two labeled products were formed; one was a glycogen-like polysaccharide and the other was a glycoprotein with glucosyl chains bound to protein through an acid-labile bond. After mild treatment of the glucoprotein with acid, the product liberated from the protein behaved as a mixture of malto-oligosaccharides and alpha-1,4-glucan with branches. The carbohydrate moiety of the glucoprotein seemed to be released upon prolonged incubation with the enzyme preparation. The glucan thus liberated from the glucoprotein may serve as a primer for the glycogen synthase. The results obtained are therefore suggestive of the existence of a glucoproteic intermediate in the initiation of glycogen biosynthesis.
|
Biosynthesis of glycogen in Neurospora crassa. Existence of a glucoproteic intermediate in the initiation process. A soluble enzyme preparation (20,000 X g supernatant fraction), prepared from the mycelia of wild-type Neurospora crassa, was capable of transferring [14C]glucose from UDP-[14C]glucose into both trichloroacetic acid (TCA)-soluble and TCA-insoluble macromolecule products in the absence of added primer. These reactions did not require either high concentrations of salts or any other chemical reagents. Two labeled products were formed; one was a glycogen-like polysaccharide and the other was a glycoprotein with glucosyl chains bound to protein through an acid-labile bond. After mild treatment of the glucoprotein with acid, the product liberated from the protein behaved as a mixture of malto-oligosaccharides and alpha-1,4-glucan with branches. The carbohydrate moiety of the glucoprotein seemed to be released upon prolonged incubation with the enzyme preparation. The glucan thus liberated from the glucoprotein may serve as a primer for the glycogen synthase. The results obtained are therefore suggestive of the existence of a glucoproteic intermediate in the initiation of glycogen biosynthesis.
|
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] |
PMID:19441
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Studies on adrenaline-induced lipolysis in artificial lipid micelles.
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Lipid micelles were prepared by incubating a mixture of glycerides (triolein, diolein, and monoolein), and lecithin in Krebs-Ringer phosphate buffer at 37 degrees C for 30 min. It was found that adrenaline stimulated the release of free fatty acids in a lipolytic system consisting of the lipid micelles and adipose tissue lipase. Adrenaline did not increase the cyclic AMP content of the reaction mixture. Dibutyryl cyclic AMP, theophylline, and phospholipase C increased the rate of lipolysis in the system but cyclic AMP and phospholipase D did not.
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Studies on adrenaline-induced lipolysis in artificial lipid micelles. Lipid micelles were prepared by incubating a mixture of glycerides (triolein, diolein, and monoolein), and lecithin in Krebs-Ringer phosphate buffer at 37 degrees C for 30 min. It was found that adrenaline stimulated the release of free fatty acids in a lipolytic system consisting of the lipid micelles and adipose tissue lipase. Adrenaline did not increase the cyclic AMP content of the reaction mixture. Dibutyryl cyclic AMP, theophylline, and phospholipase C increased the rate of lipolysis in the system but cyclic AMP and phospholipase D did not.
|
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] |
PMID:19442
|
Purification of lipase from Chromobacterium viscosum by chromatography on palmitoyl cellulose.
|
Palmitoyl cellulose was used to adsorb the extracellular lipase [triacylglycerol acyl-hydrolase EC 3.1.1.3] of Chromobacterium viscosum from crude enzyme solution, and the adsorbed enzyme was eluted with a suitable detergent, such as Adekatol 45-S-8 or Triton X-100. The enzyme was then purified by chromatography on a palmitoylated gauze column with an overall recovery of 71% and an increase in the specific activity of 11-fold from the supernatant fluid of bacterial cultures. Further purification procedures included fractionation with acetone, and chromatography on Sephadex G-150 and G-75 columns. Two isoenzymes were obtained, each in a homogeneous state on sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis: one had a molecular weight of 120,000 and pI of 3.7 and the other a molecular weight of 30,000 with a pI of 7.3.
|
Purification of lipase from Chromobacterium viscosum by chromatography on palmitoyl cellulose. Palmitoyl cellulose was used to adsorb the extracellular lipase [triacylglycerol acyl-hydrolase EC 3.1.1.3] of Chromobacterium viscosum from crude enzyme solution, and the adsorbed enzyme was eluted with a suitable detergent, such as Adekatol 45-S-8 or Triton X-100. The enzyme was then purified by chromatography on a palmitoylated gauze column with an overall recovery of 71% and an increase in the specific activity of 11-fold from the supernatant fluid of bacterial cultures. Further purification procedures included fractionation with acetone, and chromatography on Sephadex G-150 and G-75 columns. Two isoenzymes were obtained, each in a homogeneous state on sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis: one had a molecular weight of 120,000 and pI of 3.7 and the other a molecular weight of 30,000 with a pI of 7.3.
|
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] |
PMID:19443
|
A correlation between the secondary structure of DNA and the reactivity of adenine residues with chloroacetaldehyde.
|
The rate of reaction of chloroacetaldehyde (0.039 M) with the "free" adenine residue in deoxyadenosine-5'-phosphate (dAMP) at pH 6.5 has been found to be nearly equal to that at pH 4.5. Practically 100% of the adenine is converted to a fluorescent product (epsilon-adenine residue) on incubation for 60 h at 37 degrees C and pH 6.5. Of the adenine residues in "single-stranded" DNA, however, only 14% react with chloroacetaldehyde (0.039 M) under the same incubation conditions. The reaction rate of this 14% is nearly equal to that of dAMP, but the fluorescence of the product is appreciably quenched; the quantum yield is only 0.45 times that of the "free" adenine residue. In "double-helical" DNA, on the other hand, no adenine residue has been found to react with chloracetaldehyde. Possible application of these findings to structural studies of DNA is suggested.
|
A correlation between the secondary structure of DNA and the reactivity of adenine residues with chloroacetaldehyde. The rate of reaction of chloroacetaldehyde (0.039 M) with the "free" adenine residue in deoxyadenosine-5'-phosphate (dAMP) at pH 6.5 has been found to be nearly equal to that at pH 4.5. Practically 100% of the adenine is converted to a fluorescent product (epsilon-adenine residue) on incubation for 60 h at 37 degrees C and pH 6.5. Of the adenine residues in "single-stranded" DNA, however, only 14% react with chloroacetaldehyde (0.039 M) under the same incubation conditions. The reaction rate of this 14% is nearly equal to that of dAMP, but the fluorescence of the product is appreciably quenched; the quantum yield is only 0.45 times that of the "free" adenine residue. In "double-helical" DNA, on the other hand, no adenine residue has been found to react with chloracetaldehyde. Possible application of these findings to structural studies of DNA is suggested.
|
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] |
PMID:19444
|
C-Terminal peptidyl-L-proline hydrolase activity of Aspergillus acid carboxypeptidase.
|
Aspergillus saitoi acid carboxypeptidase hydrolyzed C-terminal peptidyl-L-proline bonds and released the C-terminal proline from Z-Gly-Pro-Leu-Gly-Pro and Z-Gly-Pro at pH 3.3. Proline liberated by the enzymic reaction was measured by a sensitive colorimetric ninhydrin method in glacial acetic acid at 513 nm. A Km value of 1.0 mM and a kcat value of 0.09 s-1 for Z-Gly-Pro-Leu-Gly-Pro hydrolysis, and a Km value of 5.0 mM and a kcat value of 0.0045 s-1 for Z-Gly-Pro hydrolysis were calculated from Lineweaver-Burk plots.
|
C-Terminal peptidyl-L-proline hydrolase activity of Aspergillus acid carboxypeptidase. Aspergillus saitoi acid carboxypeptidase hydrolyzed C-terminal peptidyl-L-proline bonds and released the C-terminal proline from Z-Gly-Pro-Leu-Gly-Pro and Z-Gly-Pro at pH 3.3. Proline liberated by the enzymic reaction was measured by a sensitive colorimetric ninhydrin method in glacial acetic acid at 513 nm. A Km value of 1.0 mM and a kcat value of 0.09 s-1 for Z-Gly-Pro-Leu-Gly-Pro hydrolysis, and a Km value of 5.0 mM and a kcat value of 0.0045 s-1 for Z-Gly-Pro hydrolysis were calculated from Lineweaver-Burk plots.
|
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] |
PMID:19447
|
Regulation of protein synthesis in hen's oviducts. II. Extracellular ovalbumin as an inhibitor of ovalbumin synthesis in the oviducts.
|
Washed, preincubated minced hen's oviducts, which contained low levels of extracellular and intracellular proteins, synthesized egg-white proteins actively. The addition of ovalbumin to the incubation medium resulted in inhibition of the synthesis of egg-white proteins by the washed, preincubated oviduct cells, while the addition of bovine serum albumin seemed to stimulate protein synthesis and hen's egg-white lysozyme had no effect. The inhibitory or stimulatory effect on protein synthesis was proportional to the amount of protein added to the medium. The inhibitory effect of added ovalbumin was shown not to be due to the incorporation of ovalbumin into the oviduct cells from the incubation medium. Egg-white proteins added to the medium also inhibited protein synthesis inside the cells and the extent of the inhibition appeared to correspond to the amount of ovalbumin present in egg-white.
|
Regulation of protein synthesis in hen's oviducts. II. Extracellular ovalbumin as an inhibitor of ovalbumin synthesis in the oviducts. Washed, preincubated minced hen's oviducts, which contained low levels of extracellular and intracellular proteins, synthesized egg-white proteins actively. The addition of ovalbumin to the incubation medium resulted in inhibition of the synthesis of egg-white proteins by the washed, preincubated oviduct cells, while the addition of bovine serum albumin seemed to stimulate protein synthesis and hen's egg-white lysozyme had no effect. The inhibitory or stimulatory effect on protein synthesis was proportional to the amount of protein added to the medium. The inhibitory effect of added ovalbumin was shown not to be due to the incorporation of ovalbumin into the oviduct cells from the incubation medium. Egg-white proteins added to the medium also inhibited protein synthesis inside the cells and the extent of the inhibition appeared to correspond to the amount of ovalbumin present in egg-white.
|
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] |
PMID:19450
|
Interaction of thiolsubtilisin with Streptomyces subtilisin inhibitor, SSI.
|
Subtilisin BPN' was chemically converted to thiolsubtilisin and the interaction of this modified enzyme with Streptomyces subtilisin inhibitor (SSI) was examined. SSI competitively inhibited the esterolytic activity of thiolsubtilisin toward p-nitrophenyl acetate with a K1 value of 1.3 X 10(-5) M at pH 7.5 Spectrophotometric analysis of the interaction between SSI and the modified enzyme yielded a Kd value of 4 X 10(-5) M at pH 9.7. These values are about 10(5)-fold greater than the Kd value (less than 10(-9) M at pH 7.5) for the native enzyme. This indicates that the small change in the active site structure of subtilisin (Ser221 to Cys221) leads to a considerable decrease in the binding affinity (by about 6-7 kcal/mol) to SSI.
|
Interaction of thiolsubtilisin with Streptomyces subtilisin inhibitor, SSI. Subtilisin BPN' was chemically converted to thiolsubtilisin and the interaction of this modified enzyme with Streptomyces subtilisin inhibitor (SSI) was examined. SSI competitively inhibited the esterolytic activity of thiolsubtilisin toward p-nitrophenyl acetate with a K1 value of 1.3 X 10(-5) M at pH 7.5 Spectrophotometric analysis of the interaction between SSI and the modified enzyme yielded a Kd value of 4 X 10(-5) M at pH 9.7. These values are about 10(5)-fold greater than the Kd value (less than 10(-9) M at pH 7.5) for the native enzyme. This indicates that the small change in the active site structure of subtilisin (Ser221 to Cys221) leads to a considerable decrease in the binding affinity (by about 6-7 kcal/mol) to SSI.
|
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] |
PMID:19451
|
Effects of adenosine triphosphate on N-ethylmaleimide-induced modification of 30S dynein from Tetrahymena cilia.
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Ciliary 30S dynein of Tetrahymena was investigated with regard to modification of the ATPase activity with N-ethylmaleimide (NEM) in the presence of ATP. The elevation of enzyme activity due to the modification was largely repressed by addition of ATP at a concentration of 1 mM or more during preincubation of 20 h at 0 degrees C. The repression was highly specific for ATP, though ADP and AMPPNP showed slight repressive effects. After complete hydrolysis of ATP added to the preincubation mixture, however, elevation of 30S dynein ATPase activity occurred. It is suggested that the repression by ATP of NEM-induced elevation of 30S dynein ATPase activity is simply due to a protecting effect of ATP on certain SH group(s) (probably SH1-type group(s)) around the active center of 30S dynein. When 30S dynein was maximally activated by modification with NEM, ATP or ADP did not significantly promote the inactivation of the modified enzyme upon further treatment with NEM, indicating that 30S dynein lacks the characteristics of SH2-type groups. On the other hand, ATP also showed a protective effect against inhibition of native 30S dynein by high concentrations of NEM. High concentrations of ADP and AMPPNP were inhibitory to 30S dynein ATPase activity but inorganic phosphate did not inhibit 14S or 30S dynein ATPase activities at all.
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Effects of adenosine triphosphate on N-ethylmaleimide-induced modification of 30S dynein from Tetrahymena cilia. Ciliary 30S dynein of Tetrahymena was investigated with regard to modification of the ATPase activity with N-ethylmaleimide (NEM) in the presence of ATP. The elevation of enzyme activity due to the modification was largely repressed by addition of ATP at a concentration of 1 mM or more during preincubation of 20 h at 0 degrees C. The repression was highly specific for ATP, though ADP and AMPPNP showed slight repressive effects. After complete hydrolysis of ATP added to the preincubation mixture, however, elevation of 30S dynein ATPase activity occurred. It is suggested that the repression by ATP of NEM-induced elevation of 30S dynein ATPase activity is simply due to a protecting effect of ATP on certain SH group(s) (probably SH1-type group(s)) around the active center of 30S dynein. When 30S dynein was maximally activated by modification with NEM, ATP or ADP did not significantly promote the inactivation of the modified enzyme upon further treatment with NEM, indicating that 30S dynein lacks the characteristics of SH2-type groups. On the other hand, ATP also showed a protective effect against inhibition of native 30S dynein by high concentrations of NEM. High concentrations of ADP and AMPPNP were inhibitory to 30S dynein ATPase activity but inorganic phosphate did not inhibit 14S or 30S dynein ATPase activities at all.
|
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] |
PMID:19452
|
Collagenase of human skin basal cell epithelioma.
|
Collagenase of human basal cell epithelioma was purified by sequential ammonium sulfate precipitation, Sephadex gel filtration and affinity chromatography on collagen-polyacrylamide gel. The collagenase, when partially purified, was found to have an approximate molecular weight of 50,000. The purified enzyme contained no caseinolytic activity. On polyacrylamide gel electrophoresis, the purified enzyme gave a single protein band. The purified collagenase cleaved native acid-soluble guinea pig skin collagen at 37 degrees C with a pH optimum of 8. The enzyme was inhibited by EDTA, cysteine, and human serum but not by soybean trypsin inhibitor. Heparin did not stimulate the enzyme activity. Purified collagenase reduced the specific viscosity of native acid-soluble guinea pig skin collagen to 50 per cent of its original value at 27 degrees C. Polyacrylamide gel disc electrophoresis of the reaction products showed bands corresponding to alphaA, betaA, and alphaB fragments. Electron microscopic examination of SLS aggregates of the reaction products showed that the cleavage site by the enzyme was at a point 75 per cent from the "A" end (TCA75) and 25 per cent from the "B" end (TCB25) of the collagen molecule.
|
Collagenase of human skin basal cell epithelioma. Collagenase of human basal cell epithelioma was purified by sequential ammonium sulfate precipitation, Sephadex gel filtration and affinity chromatography on collagen-polyacrylamide gel. The collagenase, when partially purified, was found to have an approximate molecular weight of 50,000. The purified enzyme contained no caseinolytic activity. On polyacrylamide gel electrophoresis, the purified enzyme gave a single protein band. The purified collagenase cleaved native acid-soluble guinea pig skin collagen at 37 degrees C with a pH optimum of 8. The enzyme was inhibited by EDTA, cysteine, and human serum but not by soybean trypsin inhibitor. Heparin did not stimulate the enzyme activity. Purified collagenase reduced the specific viscosity of native acid-soluble guinea pig skin collagen to 50 per cent of its original value at 27 degrees C. Polyacrylamide gel disc electrophoresis of the reaction products showed bands corresponding to alphaA, betaA, and alphaB fragments. Electron microscopic examination of SLS aggregates of the reaction products showed that the cleavage site by the enzyme was at a point 75 per cent from the "A" end (TCA75) and 25 per cent from the "B" end (TCB25) of the collagen molecule.
|
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0.02258678711950779,
-0.04886661842465401,
0.11565171927213669,
0.05518180504441261
] |
PMID:19453
|
alpha-chymotrypsin-catalyzed hydrolysis of phenyl acetate. Large Hammett's rho constant and participation of histidine-acylated intermediate.
|
A detailed examination of the mechanism of the hydrolysis of phenyl acetates by alpha-chymotrypsin [EC 3.4.21.1] was carried out. The effective deacylation rate constants of some phenyl acetates obtained by titration of the acetyl-enzyme decreased at low substrate concentrations and showed anomalous pH dependences and solvent isotope effects. The transient kinetics of deacylation of the acetyl-enzyme were biphasic. A spectrum and a breakdown rate similar to those of acetylimidazole were observed when the acetyl-enzyme was denaturated with sodium dodecyl sulfate. These results indicate the participation of histidine-acylated enzyme, which woud account for the anomalous phenomena previously found in this system, including a large value of Hammett's rho. The relation between the substrate activation and the two intermediates is discussed.
|
alpha-chymotrypsin-catalyzed hydrolysis of phenyl acetate. Large Hammett's rho constant and participation of histidine-acylated intermediate. A detailed examination of the mechanism of the hydrolysis of phenyl acetates by alpha-chymotrypsin [EC 3.4.21.1] was carried out. The effective deacylation rate constants of some phenyl acetates obtained by titration of the acetyl-enzyme decreased at low substrate concentrations and showed anomalous pH dependences and solvent isotope effects. The transient kinetics of deacylation of the acetyl-enzyme were biphasic. A spectrum and a breakdown rate similar to those of acetylimidazole were observed when the acetyl-enzyme was denaturated with sodium dodecyl sulfate. These results indicate the participation of histidine-acylated enzyme, which woud account for the anomalous phenomena previously found in this system, including a large value of Hammett's rho. The relation between the substrate activation and the two intermediates is discussed.
|
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] |
PMID:19454
|
The occurence of a neutral protease and its inhibitor in rat peritoneal macrophages.
|
The lysate of the glycogen-induced macrophages in rat peritoneal exudate was fractionated by centrifugation and extraction into a water extract, 1 M KCl extract and residue fractions. Approximately 50% of the neutral protease activity toward casein in the lysate was recovered in the KCl extract fraction, which was practically devoid of acid protease, cathepsin D. The pH optimum of the neutral protease toward casein and urea-denatured hemoglobin was pH 8.5. The activity was inhibited strongly by DFP or chymostatin and only partially by HgCl2 or PCMB. Addition of a salt to the reaction medium caused enhancement of the activity with an optimum concentration of 0.25 M: KCl, KBr, KI, NaCl, NaBr, NaI, and MgCl2 were all almost equally effective. When the enzyme preparation was filtered through a column of Sephadex G-75 gel in the presence of 1 M KCl, a larger molecular weight fraction at the void volume was obtained in addition to a smaller molecular weight fraction showing a caseinolytic activity insensitive to KCl concentration. The former was found to have a specific inhibitory effect on the latter activity.
|
The occurence of a neutral protease and its inhibitor in rat peritoneal macrophages. The lysate of the glycogen-induced macrophages in rat peritoneal exudate was fractionated by centrifugation and extraction into a water extract, 1 M KCl extract and residue fractions. Approximately 50% of the neutral protease activity toward casein in the lysate was recovered in the KCl extract fraction, which was practically devoid of acid protease, cathepsin D. The pH optimum of the neutral protease toward casein and urea-denatured hemoglobin was pH 8.5. The activity was inhibited strongly by DFP or chymostatin and only partially by HgCl2 or PCMB. Addition of a salt to the reaction medium caused enhancement of the activity with an optimum concentration of 0.25 M: KCl, KBr, KI, NaCl, NaBr, NaI, and MgCl2 were all almost equally effective. When the enzyme preparation was filtered through a column of Sephadex G-75 gel in the presence of 1 M KCl, a larger molecular weight fraction at the void volume was obtained in addition to a smaller molecular weight fraction showing a caseinolytic activity insensitive to KCl concentration. The former was found to have a specific inhibitory effect on the latter activity.
|
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] |
PMID:19455
|
Interactions of alpha-chymotrypsin with peptides containing tryptophan or its derivatives at the C-terminus.
|
The interaction between alpha-chymotrypsin [EC 3.4.21.1] and peptide substrate or peptide inhibitor was investigated to determine how the secondary interaction influences the rate of hydrolysis or the binding and whether or not its effect is variable with alteration of the P1 residue which interacts with the specificity determining site of the enzyme. Kinetic analysis was carried out at pH 6.5 and 7.8 for substrates of the type Ac-Glyn-X-OMe and for inhibitors of the type Ac-Glyn-X-OH where X denotes tryptophan or its derivatives. With substrates containing tryptophan or Nin-formyltryptophan, the second-order rate of hydrolysis increases with increase of chain length. With substrates containing 2-(2-nitro-4-carboxyphenylsulfenyl)-tryptophan, however, the rate of hydrolysis decreases with elongation of the chain, due to an increase in Km(app). The corresponding inhibitors behave differently from the other series of inhibitors at pH 6.5. The results indicate that the influence of the secondary interaction on reactivity or binding is related to the structural features of the P1 residue.
|
Interactions of alpha-chymotrypsin with peptides containing tryptophan or its derivatives at the C-terminus. The interaction between alpha-chymotrypsin [EC 3.4.21.1] and peptide substrate or peptide inhibitor was investigated to determine how the secondary interaction influences the rate of hydrolysis or the binding and whether or not its effect is variable with alteration of the P1 residue which interacts with the specificity determining site of the enzyme. Kinetic analysis was carried out at pH 6.5 and 7.8 for substrates of the type Ac-Glyn-X-OMe and for inhibitors of the type Ac-Glyn-X-OH where X denotes tryptophan or its derivatives. With substrates containing tryptophan or Nin-formyltryptophan, the second-order rate of hydrolysis increases with increase of chain length. With substrates containing 2-(2-nitro-4-carboxyphenylsulfenyl)-tryptophan, however, the rate of hydrolysis decreases with elongation of the chain, due to an increase in Km(app). The corresponding inhibitors behave differently from the other series of inhibitors at pH 6.5. The results indicate that the influence of the secondary interaction on reactivity or binding is related to the structural features of the P1 residue.
|
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0.022612938657402992,
0.004787683021277189,
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0.07345866411924362,
0.017749177291989326,
-0.04360788315534592,
0.06228402256965637,
0.0341070182621479
] |
PMID:19457
|
Purification and properties of aldehyde dehydrogenase from Saccharomyces cerevisiae.
|
A procedure for the purification of aldehyde dehydrogenase from bakers' yeast (Saccharomyces cerevisiae) is reported. Treatment with acid, heat and organic solvents was avoided and chromatographic and filtration techniques in the presence of phenylmethylsulfonylfluoride were mainly used. An affinity chromatography step using the reactive dye Cibacron blue F3G-A, which was covalently bound to Sepharose 4B, was found to be essential. The enzyme was bound to and then released from the dye. The purified enzyme was shown to be homogeneous by gel filtration, disc electrophoresis and SDS electrophoresis. The molecular weight of the purified enzyme determined by gel filtration was 170,000, which agreed with that of the enzyme in the crude extract. The enzyme was composed of subunits of a molecular weight of 57,000. The specific activity of the enzyme was 20 units per mg of protein under the standard assay conditions. The substrate specificity, the relative maximal velocity, the michaelis constants, the pH optimum, the stability and the activation energy of the enzyme are reported.
|
Purification and properties of aldehyde dehydrogenase from Saccharomyces cerevisiae. A procedure for the purification of aldehyde dehydrogenase from bakers' yeast (Saccharomyces cerevisiae) is reported. Treatment with acid, heat and organic solvents was avoided and chromatographic and filtration techniques in the presence of phenylmethylsulfonylfluoride were mainly used. An affinity chromatography step using the reactive dye Cibacron blue F3G-A, which was covalently bound to Sepharose 4B, was found to be essential. The enzyme was bound to and then released from the dye. The purified enzyme was shown to be homogeneous by gel filtration, disc electrophoresis and SDS electrophoresis. The molecular weight of the purified enzyme determined by gel filtration was 170,000, which agreed with that of the enzyme in the crude extract. The enzyme was composed of subunits of a molecular weight of 57,000. The specific activity of the enzyme was 20 units per mg of protein under the standard assay conditions. The substrate specificity, the relative maximal velocity, the michaelis constants, the pH optimum, the stability and the activation energy of the enzyme are reported.
|
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] |
PMID:19458
|
Effects of phthalate esters on the latent ATPase and swelling of mitochondria.
|
Phthalate esters have shown to stimulate the latent ATPase [EC 3.6.1.3] activity and induce mitochondrial swelling. Among the tested phthalate esters, di-n-butyl phthalate (DBP) exhibited the greatest activity, and the activity decreased progressively as the alkyl chain was lengthened or shortened. The DBP-stimulated ATPase was oligomycin-sensitive. The degree of stimulation of the ATPase was proportional to the extent of mitochondrial swelling induced by DBP in 0.1 M Tris-HCl (pH 7.2) containing 0.25 M sucrose. However, the swelling was dependent on the tonicity of the solution or the concentration of chloride ions, while the stimulation of ATPase was independent of these factors. Swelling was strongly induced by DBP at slightly acidic rather than neutral or alkaline pH. The pH-activity curve of DBP-stimulated ATPase was in inverse correlation with that of swelling, which showed a rather flat maximum at pH 8.0. When bovine serum albumin (BSA) was added to a solution containing mitochondria before addition of DBP, swelling was no longer caused by DBP, though the latent ATPase was stimulated to the same extent in the absence of added BSA.
|
Effects of phthalate esters on the latent ATPase and swelling of mitochondria. Phthalate esters have shown to stimulate the latent ATPase [EC 3.6.1.3] activity and induce mitochondrial swelling. Among the tested phthalate esters, di-n-butyl phthalate (DBP) exhibited the greatest activity, and the activity decreased progressively as the alkyl chain was lengthened or shortened. The DBP-stimulated ATPase was oligomycin-sensitive. The degree of stimulation of the ATPase was proportional to the extent of mitochondrial swelling induced by DBP in 0.1 M Tris-HCl (pH 7.2) containing 0.25 M sucrose. However, the swelling was dependent on the tonicity of the solution or the concentration of chloride ions, while the stimulation of ATPase was independent of these factors. Swelling was strongly induced by DBP at slightly acidic rather than neutral or alkaline pH. The pH-activity curve of DBP-stimulated ATPase was in inverse correlation with that of swelling, which showed a rather flat maximum at pH 8.0. When bovine serum albumin (BSA) was added to a solution containing mitochondria before addition of DBP, swelling was no longer caused by DBP, though the latent ATPase was stimulated to the same extent in the absence of added BSA.
|
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] |
PMID:19459
|
Properties of soluble rat brain histone lysine methyltransferase.
|
Histone-lysine methyltransferase has been solubilized from rat brain chromatin by repeated extraction with distilled water. The enzyme was further purified by chromatography on DEAE-cellulose and gel filtration. With chromosomal-bound histones as substrates, the enzyme methylated only the lysyl residues in histones H3 and H4. The ratio of N epsilon-mono-: N epsilon-di-: N epsilon-trimethyllysine in histone H3 was 1.8:1.0:0.45 and the ratio of N epsilon-mono-: N epsilon-dimethyllysine in histone H4 was 0.7:1.0. The enzyme loses specificity with soluble histones as substrates; however, histones H3 and H4 were still the best methyl acceptors. The pH optima for the enzyme with soluble histones H3 and H4 as substrates were 8.2 to 8.7 and 7.2 to 8.0, respectively. S-Adenosyl-L-homocysteine, one of the products of the reaction, was a competitive inhibitor with respect to S-adenosyl-L-methionine.
|
Properties of soluble rat brain histone lysine methyltransferase. Histone-lysine methyltransferase has been solubilized from rat brain chromatin by repeated extraction with distilled water. The enzyme was further purified by chromatography on DEAE-cellulose and gel filtration. With chromosomal-bound histones as substrates, the enzyme methylated only the lysyl residues in histones H3 and H4. The ratio of N epsilon-mono-: N epsilon-di-: N epsilon-trimethyllysine in histone H3 was 1.8:1.0:0.45 and the ratio of N epsilon-mono-: N epsilon-dimethyllysine in histone H4 was 0.7:1.0. The enzyme loses specificity with soluble histones as substrates; however, histones H3 and H4 were still the best methyl acceptors. The pH optima for the enzyme with soluble histones H3 and H4 as substrates were 8.2 to 8.7 and 7.2 to 8.0, respectively. S-Adenosyl-L-homocysteine, one of the products of the reaction, was a competitive inhibitor with respect to S-adenosyl-L-methionine.
|
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-0.01758033037185669,
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-0.01962929405272007,
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0.02094438299536705
] |
PMID:19462
|
Investigation of the relation of the pH-dependent dissociation of malate dehydrogenase to modification of the enzyme by N-ethylmaleimide.
|
The pH-dependent dissociation of porcine heart mitochondrial malate dehydrogenase (L-malate:NAD+ oxidoreductase, EC 1.1.1.37) has been further characterized using the technique of sedimentation velocity ultracentrifugation. The increased rate and specificity of the inactivation of mitochondrial malate dehydrogenase by the sulfhydryl reagent N-ethylmaleimide has been correlated with the pH-dependent dissociation of the enzyme. Data obtained using NAD+ and its component parts to reassociate the enzyme and also to protect the enzyme from inactivation by N-ethylmaleimide suggest that the sulfhydryl residues being modified by N-ethylmaleimide are inaccessible when the enzyme is in its dimeric form. A dissociation curve for the pH-dependent dissociation suggests that a limited number of residues are being protonated concomitant with dissociation of the enzyme. An apparent pKa of 5.3 has been determined for this phenomenon. Studies using enzyme modified by the sulfhydryl reagent N-ethylmaleimide indicate that selective modification of essential sulfhydryl residues alters the proper binding of NADH.
|
Investigation of the relation of the pH-dependent dissociation of malate dehydrogenase to modification of the enzyme by N-ethylmaleimide. The pH-dependent dissociation of porcine heart mitochondrial malate dehydrogenase (L-malate:NAD+ oxidoreductase, EC 1.1.1.37) has been further characterized using the technique of sedimentation velocity ultracentrifugation. The increased rate and specificity of the inactivation of mitochondrial malate dehydrogenase by the sulfhydryl reagent N-ethylmaleimide has been correlated with the pH-dependent dissociation of the enzyme. Data obtained using NAD+ and its component parts to reassociate the enzyme and also to protect the enzyme from inactivation by N-ethylmaleimide suggest that the sulfhydryl residues being modified by N-ethylmaleimide are inaccessible when the enzyme is in its dimeric form. A dissociation curve for the pH-dependent dissociation suggests that a limited number of residues are being protonated concomitant with dissociation of the enzyme. An apparent pKa of 5.3 has been determined for this phenomenon. Studies using enzyme modified by the sulfhydryl reagent N-ethylmaleimide indicate that selective modification of essential sulfhydryl residues alters the proper binding of NADH.
|
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] |
PMID:19463
|
Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit.
|
Human kidney gamma-glutamyl transpeptidase has been purified by a procedure involving Lubrol extraction, acetone precipitation, treatment with bromelain, and column chromatography on DEAE-cellulose and Sephadex G-150. The final preparation is a glycoprotein (molecular weight of approximately 84,000) composed of two nonidentical glycopeptides (molecular weights of 62,000 and 22,000). The isozymic forms, separable by isoelectric focusing, have different contents of sialic acid. The utilization of L-glutamine (which is both a gamma-glutamyl donor and acceptor) is stimulated about 3-fold by maleate in contrast to 10-fold stimulation of glutamine utilization by the rat kidney enzyme. The gamma-glutamyl analogs, 6-diazo-5-oxo-L-norleucine (DON) and L-azaserine inactivate the human kidney enzyme with respect to its transpeptidase and hydrolase activities. Inactivation is prevented by gamma-glutamyl substrates (but not by acceptor substrates) and is accelerated by maleate. [14C]DON reacts covalently and stoichiometrically at the gamma-glutamyl site, which was localized to the light subunit of the enzyme. The light subunit of human transpeptidase closely resembles that of rat kidney enzyme in having the gamma-glutamyl binding site, and similar molecular weight and amino acid composition. The heavy subunits of the two enzymes are markedly different in both molecular weight and amino acid content; this may account for differences observed in acceptor amino acid specificity and in the magnitude of the maleate effect.
|
Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit. Human kidney gamma-glutamyl transpeptidase has been purified by a procedure involving Lubrol extraction, acetone precipitation, treatment with bromelain, and column chromatography on DEAE-cellulose and Sephadex G-150. The final preparation is a glycoprotein (molecular weight of approximately 84,000) composed of two nonidentical glycopeptides (molecular weights of 62,000 and 22,000). The isozymic forms, separable by isoelectric focusing, have different contents of sialic acid. The utilization of L-glutamine (which is both a gamma-glutamyl donor and acceptor) is stimulated about 3-fold by maleate in contrast to 10-fold stimulation of glutamine utilization by the rat kidney enzyme. The gamma-glutamyl analogs, 6-diazo-5-oxo-L-norleucine (DON) and L-azaserine inactivate the human kidney enzyme with respect to its transpeptidase and hydrolase activities. Inactivation is prevented by gamma-glutamyl substrates (but not by acceptor substrates) and is accelerated by maleate. [14C]DON reacts covalently and stoichiometrically at the gamma-glutamyl site, which was localized to the light subunit of the enzyme. The light subunit of human transpeptidase closely resembles that of rat kidney enzyme in having the gamma-glutamyl binding site, and similar molecular weight and amino acid composition. The heavy subunits of the two enzymes are markedly different in both molecular weight and amino acid content; this may account for differences observed in acceptor amino acid specificity and in the magnitude of the maleate effect.
|
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] |
PMID:19464
|
Steady state and equilibrium exchange kinetic studies of the sheep brain glutamine synthetase reaction.
|
The kinetic mechanism of the sheep brain glutamine synthetase has been examined by both initial rate kinetics using the glutamate analog beta-glutamate and by isotope exchange measurements at equilibrium. Results of the initial rate studies were compatible with a number of sequential mechanisms but not with a partially or fully ordered rapid equilibrium or a ping-pong mechanism. Kinetic parameters at 37 degrees and pH 7.2 were K beta-Glu = 16 mM, KATP = 0.28 mM, and KNH2OH = 1.4 mM. For all equilibrium exchanges studied (ATP in equilibrium ADP, ATP in equilibrium Pi, and Glu in equilibrium Gln), the rate of exchange rose smoothly to a maximum as all substrates and products were simultaneously raised in a constant ratio. This result is in accord with a random order of substrate addition. A brief treatment of equilibrium exchange rates in cases where all substrate/product pairs are varied together is also presented.
|
Steady state and equilibrium exchange kinetic studies of the sheep brain glutamine synthetase reaction. The kinetic mechanism of the sheep brain glutamine synthetase has been examined by both initial rate kinetics using the glutamate analog beta-glutamate and by isotope exchange measurements at equilibrium. Results of the initial rate studies were compatible with a number of sequential mechanisms but not with a partially or fully ordered rapid equilibrium or a ping-pong mechanism. Kinetic parameters at 37 degrees and pH 7.2 were K beta-Glu = 16 mM, KATP = 0.28 mM, and KNH2OH = 1.4 mM. For all equilibrium exchanges studied (ATP in equilibrium ADP, ATP in equilibrium Pi, and Glu in equilibrium Gln), the rate of exchange rose smoothly to a maximum as all substrates and products were simultaneously raised in a constant ratio. This result is in accord with a random order of substrate addition. A brief treatment of equilibrium exchange rates in cases where all substrate/product pairs are varied together is also presented.
|
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0.0506749153137207,
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] |
PMID:19467
|
Purified proton conductor in proton translocating adenosine triphosphatase of a thermophilic bacterium.
|
1. The membrane-integrated portion (TF0) of the proton translocating ATPase complex (TF0-F1) of the thermophilic bacterium PS3 was highly purified. Its proton-conducting activity was investigated in vesicles reconstituted from TF0 and phospholipids (TF0 vesicles). 2. The rate of proton conduction through TF0 was proportional to the membrane potential imposed (6H+ uptake/s/TF0 molecule with 103 mV at pH 8.0). The pH profile of the rate revealed that a proton, not a hydroxy ion, was the true substrate conducted and that there was a monoprotic proton binding site in TF0 (pKa = 6.8). The temperature coefficient of proton conductance of TF0 showed a considerable variation depending on the phospholipids of the vesicles with respective transition temperatures. 3. Passive proton conduction through TF0 was inhibited stoichiometrically by addition of either the soluble ATPase portion (TF1) of TF0-F1, or an energy transfer inhibitor dicyclohexylcarbodiimide or an antibody against TF0. 4. The proton conductance of TF0 was concluded to represent its intrinsic activity in the original TF0-F1 complex.
|
Purified proton conductor in proton translocating adenosine triphosphatase of a thermophilic bacterium. 1. The membrane-integrated portion (TF0) of the proton translocating ATPase complex (TF0-F1) of the thermophilic bacterium PS3 was highly purified. Its proton-conducting activity was investigated in vesicles reconstituted from TF0 and phospholipids (TF0 vesicles). 2. The rate of proton conduction through TF0 was proportional to the membrane potential imposed (6H+ uptake/s/TF0 molecule with 103 mV at pH 8.0). The pH profile of the rate revealed that a proton, not a hydroxy ion, was the true substrate conducted and that there was a monoprotic proton binding site in TF0 (pKa = 6.8). The temperature coefficient of proton conductance of TF0 showed a considerable variation depending on the phospholipids of the vesicles with respective transition temperatures. 3. Passive proton conduction through TF0 was inhibited stoichiometrically by addition of either the soluble ATPase portion (TF1) of TF0-F1, or an energy transfer inhibitor dicyclohexylcarbodiimide or an antibody against TF0. 4. The proton conductance of TF0 was concluded to represent its intrinsic activity in the original TF0-F1 complex.
|
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] |
PMID:19468
|
Manganese cytochrome c. Structure and properties.
|
Oxidized and reduced manganese cytochromes c, Mn Cyt c+ and Mn Cyt c, have been synthesized. Mn Cyt c+ and Fe Cyt c+ have identical electrophoretic and ion exchange mobilities. Mn Cyt c+ does not bind F-, CN-, or N3- ions; Mn Cyt c does not bind CO or O2. Mn Cyt c is very rapidly autooxidized by O2 even at -50 degrees. The manganese ion is readily dissociated from Mn Cyt c at acidic pH values. Both Mn Cyt c and Mn Cyt c+ are high spin complexes with 3d5 S = 5/2 and 3d4 S = 2 electronic configurations, respectively. The epr spectrum of Mn Cyt c is rhombic with (formula: see text). Both oxidized and reduced Mn Cyt c react with NO; the former reaction is reversible and the product has the following epr spectral parameters: (formula: see text). There is no superhyperfine interaction observable with the NO ligand, and the unpaired electron density is estimated to be mostly in the metal ion d xy orbital. The structure is best formulated as Mn Cyt c (NO)+. The half-reduction potential of Mn Cyt c is + 60 +/- 40 mV. It is neither oxidized by cytochrome oxidase nor reduced by NADH, NADPH, or succinate cytochrome reductase. These physical, chemical, and enzymic properties of manganese cytochromes c suggest a five-coordinate metalloporphyrin prosthetic group with the manganese ion situated significantly out-of-plane toward the side of His-18.
|
Manganese cytochrome c. Structure and properties. Oxidized and reduced manganese cytochromes c, Mn Cyt c+ and Mn Cyt c, have been synthesized. Mn Cyt c+ and Fe Cyt c+ have identical electrophoretic and ion exchange mobilities. Mn Cyt c+ does not bind F-, CN-, or N3- ions; Mn Cyt c does not bind CO or O2. Mn Cyt c is very rapidly autooxidized by O2 even at -50 degrees. The manganese ion is readily dissociated from Mn Cyt c at acidic pH values. Both Mn Cyt c and Mn Cyt c+ are high spin complexes with 3d5 S = 5/2 and 3d4 S = 2 electronic configurations, respectively. The epr spectrum of Mn Cyt c is rhombic with (formula: see text). Both oxidized and reduced Mn Cyt c react with NO; the former reaction is reversible and the product has the following epr spectral parameters: (formula: see text). There is no superhyperfine interaction observable with the NO ligand, and the unpaired electron density is estimated to be mostly in the metal ion d xy orbital. The structure is best formulated as Mn Cyt c (NO)+. The half-reduction potential of Mn Cyt c is + 60 +/- 40 mV. It is neither oxidized by cytochrome oxidase nor reduced by NADH, NADPH, or succinate cytochrome reductase. These physical, chemical, and enzymic properties of manganese cytochromes c suggest a five-coordinate metalloporphyrin prosthetic group with the manganese ion situated significantly out-of-plane toward the side of His-18.
|
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] |
PMID:19470
|
Cobalt-substituted horseradish peroxidase.
|
Horseradish peroxidase can be reconstituted with cobalt porphyrin to give a cobaltic holoenzyme having physicochemical properties quite similar to those of the native ferric protein. The cobaltic protein (Co3+HRP) can be reduced to the cobaltous form (CoHRP), the analogue of ferroperoxidase and the reduced cobalt protein can bind O2 to form an analogue of oxyferroperoxidase (Compound III). Since both the CoHRP and oxy-CoHRP are EPR-visible, the cobalt has been used to probe the nature of the heme crevice in these two protein forms. The occurrence of a three-line 14N superhyperfine pattern in the spectrum of the former unambiguously shows that in the divalent state of the protein the proximal axial ligand is a nitrogenous base. The spectrum of the latter shows a uniquely large Aparallel(59Co) = 23.2 G. Although we confirm the reported failure of the Co3+HRP to catalyze peroxide-dependent oxidations of classical peroxidase substrates (Gjessing, E.C., and Sumner, J.B. (1942) Arch. Biochem. 1, 1), the oxy-CoHRP does undergo oxidation-reduction reactions analogous to those exhibited in the cytochrome P-450 catalytic cycle.
|
Cobalt-substituted horseradish peroxidase. Horseradish peroxidase can be reconstituted with cobalt porphyrin to give a cobaltic holoenzyme having physicochemical properties quite similar to those of the native ferric protein. The cobaltic protein (Co3+HRP) can be reduced to the cobaltous form (CoHRP), the analogue of ferroperoxidase and the reduced cobalt protein can bind O2 to form an analogue of oxyferroperoxidase (Compound III). Since both the CoHRP and oxy-CoHRP are EPR-visible, the cobalt has been used to probe the nature of the heme crevice in these two protein forms. The occurrence of a three-line 14N superhyperfine pattern in the spectrum of the former unambiguously shows that in the divalent state of the protein the proximal axial ligand is a nitrogenous base. The spectrum of the latter shows a uniquely large Aparallel(59Co) = 23.2 G. Although we confirm the reported failure of the Co3+HRP to catalyze peroxide-dependent oxidations of classical peroxidase substrates (Gjessing, E.C., and Sumner, J.B. (1942) Arch. Biochem. 1, 1), the oxy-CoHRP does undergo oxidation-reduction reactions analogous to those exhibited in the cytochrome P-450 catalytic cycle.
|
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] |
PMID:19472
|
Purification from hamster cells of the multifunctional protein that initiates de novo synthesis of pyrimidine nucleotides.
|
Carbamyl-P synthetase (EC 2.7.2.9), aspartate transcarbamylase (EC 2.1.3.2), and dihydro-orotase (EC 3.5.2.3), the first three enzymes of the de novo pathway for synthesis of pyrimidine nucleotides, have been co-purified as a single oligomeric protein from a mutant line of hamster cells selected for its ability to resist N-(phosphonacetyl)-L-aspartate (PALA), a potent and specific inhibitor of aspartate transcarbamylase. All three enzymes overaccum,late in the mutant cells (Kempe, T.D., Swyryd, E.A., Bruist, M., and Stark, G.R. (1976) Cell 9, 541-550) and the oligomer represents nearly 10% of the total cellular protein. Tens of milligrams of oligomer have been purified to homogeneity by a simple and rapid procedure, with recovery of about 50% of all three activities. The pure protein contains only one size of polypeptide, Mr approximately 200,000, as revealed by electrophoresis in danaturing gels. All three enzyme activities are associated with this polypeptide, indicating that it is multifunctional. Further evidence for a multifunctional protein is provided by titration of the oligomer with radioactive PALA, which reveals that the number of PALA binding sites approximately equals the number of polypeptide chains. The isolated multifunctional protein is a mixture of trimers and hexamers.
|
Purification from hamster cells of the multifunctional protein that initiates de novo synthesis of pyrimidine nucleotides. Carbamyl-P synthetase (EC 2.7.2.9), aspartate transcarbamylase (EC 2.1.3.2), and dihydro-orotase (EC 3.5.2.3), the first three enzymes of the de novo pathway for synthesis of pyrimidine nucleotides, have been co-purified as a single oligomeric protein from a mutant line of hamster cells selected for its ability to resist N-(phosphonacetyl)-L-aspartate (PALA), a potent and specific inhibitor of aspartate transcarbamylase. All three enzymes overaccum,late in the mutant cells (Kempe, T.D., Swyryd, E.A., Bruist, M., and Stark, G.R. (1976) Cell 9, 541-550) and the oligomer represents nearly 10% of the total cellular protein. Tens of milligrams of oligomer have been purified to homogeneity by a simple and rapid procedure, with recovery of about 50% of all three activities. The pure protein contains only one size of polypeptide, Mr approximately 200,000, as revealed by electrophoresis in danaturing gels. All three enzyme activities are associated with this polypeptide, indicating that it is multifunctional. Further evidence for a multifunctional protein is provided by titration of the oligomer with radioactive PALA, which reveals that the number of PALA binding sites approximately equals the number of polypeptide chains. The isolated multifunctional protein is a mixture of trimers and hexamers.
|
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] |
PMID:19473
|
Activation by phosphate of yeast phosphofructokinase.
|
The activity of yeast phosphofructokinase assayed in vitro at physiological concentrations of known substrates and effectors is 100-fold lower than the glycolytic flux observed in vivo. Phosphate synergistically with AMP activates the enzyme to a level within the range of the physiological needs. The activation by phosphate is pH-dependent: the activation is 100-fold at pH 6.4 while no effect is observed at pH 7.5. The activation by AMP, phosphate, or both together is primarily due to changes in the affinity of the enzyme for fructose-6-P. Under conditions similar to those prevailing in glycolysing yeast (pH 6.4, 1 mM ATP, 10 mM NH4+) the apparent affinity constant for fructose-6-P (S0.5) decreases from 3 to 1.4 mM upon addition of 1 mM AMP or 10 mM phosphate; if both activators are present together, S0.5 is further decreased to 0.2 mM. In all cases the cooperativity toward fructose-6-P remains unchanged. These results are consistent with a model for phosphofructokinase where two conformations, with different affinities for fructose-6-P and ATP, will present the same affinity for AMP and phosphate. AMP would diminish the affinity for ATP at the regulatory site and phosphate would increase the affinity for fructose-6-P. The results obtained indicate that the activity of phosphofructokinase in the shift glycolysis-gluconeogenesis is mainly regulated by changes in the concentration of fructose-6-P.
|
Activation by phosphate of yeast phosphofructokinase. The activity of yeast phosphofructokinase assayed in vitro at physiological concentrations of known substrates and effectors is 100-fold lower than the glycolytic flux observed in vivo. Phosphate synergistically with AMP activates the enzyme to a level within the range of the physiological needs. The activation by phosphate is pH-dependent: the activation is 100-fold at pH 6.4 while no effect is observed at pH 7.5. The activation by AMP, phosphate, or both together is primarily due to changes in the affinity of the enzyme for fructose-6-P. Under conditions similar to those prevailing in glycolysing yeast (pH 6.4, 1 mM ATP, 10 mM NH4+) the apparent affinity constant for fructose-6-P (S0.5) decreases from 3 to 1.4 mM upon addition of 1 mM AMP or 10 mM phosphate; if both activators are present together, S0.5 is further decreased to 0.2 mM. In all cases the cooperativity toward fructose-6-P remains unchanged. These results are consistent with a model for phosphofructokinase where two conformations, with different affinities for fructose-6-P and ATP, will present the same affinity for AMP and phosphate. AMP would diminish the affinity for ATP at the regulatory site and phosphate would increase the affinity for fructose-6-P. The results obtained indicate that the activity of phosphofructokinase in the shift glycolysis-gluconeogenesis is mainly regulated by changes in the concentration of fructose-6-P.
|
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] |
PMID:19475
|
Purification and properties of a T4 bacteriophage factor that modifies valyl-tRNA synthetase of Escherichia coli.
|
After T4 bacteriophage infects Escherichia coli, a peptide tau, produced under the control of a phage gene, binds to the host valyl transfer ribonucleic acid synthetase (EC 6.1.1.9) and thereby changes several of its physicochemical properties. The interaction of tau with the host enzyme was investigated in vitro after extensively purifying the factor from T4-infected E. coli using a rapid purification procedure. The tau preparation migrated as a single, protein-staining band with a molecular weight of 11,000 during sodium dodecyl sulfate-gel electrophoresis. The purified peptide completely converted partially purified valyl-tRNA synthetase from uninfected E. coli into the form present in cell-free extracts prepared from virus-infected bacteria. The enzyme modified in vitro also exhibited the enhanced affinity for tRNA characteristic of the viral form of valyl-tRNA synthetase. The addition of bulk tRNA from E. coli B, tRNAVal, or tRNA1Val to enzyme modified in vitro increased its sedimentation rate to that of enzyme prepared from phage-infected cells. Amino acid analysis of the purified tau peptide revealed a relatively high concentration of the amino acids lysine and alanine, and a lack of detectable proline, tyrosine, phenylalanine, and methionine.
|
Purification and properties of a T4 bacteriophage factor that modifies valyl-tRNA synthetase of Escherichia coli. After T4 bacteriophage infects Escherichia coli, a peptide tau, produced under the control of a phage gene, binds to the host valyl transfer ribonucleic acid synthetase (EC 6.1.1.9) and thereby changes several of its physicochemical properties. The interaction of tau with the host enzyme was investigated in vitro after extensively purifying the factor from T4-infected E. coli using a rapid purification procedure. The tau preparation migrated as a single, protein-staining band with a molecular weight of 11,000 during sodium dodecyl sulfate-gel electrophoresis. The purified peptide completely converted partially purified valyl-tRNA synthetase from uninfected E. coli into the form present in cell-free extracts prepared from virus-infected bacteria. The enzyme modified in vitro also exhibited the enhanced affinity for tRNA characteristic of the viral form of valyl-tRNA synthetase. The addition of bulk tRNA from E. coli B, tRNAVal, or tRNA1Val to enzyme modified in vitro increased its sedimentation rate to that of enzyme prepared from phage-infected cells. Amino acid analysis of the purified tau peptide revealed a relatively high concentration of the amino acids lysine and alanine, and a lack of detectable proline, tyrosine, phenylalanine, and methionine.
|
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] |
PMID:19477
|
A sodium-specific membrane permeability defect induced by phospholipid vesicle treatment of erythrocytes.
|
Treatment of human erythrocytes with phospholipid vesicles induces a selective membrane permeability defect which leads to osmotic lysis. The defective cells exhibit a massive sodium ion leak while maintaining normal impermeability to other cations, anions, and neutral small molecules. The sodium ion influx and resulting hemolysis may be inhibited by increased pH, by tetrodotoxin, and by reintroduction of vesicle-extracted proteins into the cell. These characteristics suggest that phospholipid vesicle treatment destroys the cell by disrupting a membrane protein system involved in regulation of cation permeability.
|
A sodium-specific membrane permeability defect induced by phospholipid vesicle treatment of erythrocytes. Treatment of human erythrocytes with phospholipid vesicles induces a selective membrane permeability defect which leads to osmotic lysis. The defective cells exhibit a massive sodium ion leak while maintaining normal impermeability to other cations, anions, and neutral small molecules. The sodium ion influx and resulting hemolysis may be inhibited by increased pH, by tetrodotoxin, and by reintroduction of vesicle-extracted proteins into the cell. These characteristics suggest that phospholipid vesicle treatment destroys the cell by disrupting a membrane protein system involved in regulation of cation permeability.
|
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] |
PMID:19480
|
Interrelationship of carbohydrate metabolism and alkaline phosphatase synthesis in Bacillus licheniformis 749/c.
|
Membrane-bound alkaline phosphatase of Bacillus licheniformis 749/c is derepressed by glucose in complex and chemically defined media. In the presence of lactate, pyruvate, or succinate the synthesis is repressed. The lactate repression neither affects total protein synthesis nor inhibits penicillinase synthesis. Thus, carbon sources specifically influence alkaline phosphatase synthesis. Although variations in the inorganic phosphate content of the growth media directly affect alkaline phosphatase synthesis, the intracellular inorganic and total phosphate pools appear to be unrelated to its repression or derepression. During lactate repression there is preferential incorporation of lactate molecules into glycogen, whereas no such incorporation could be detected from glucose. Net glycogen synthesis remains the same in glucose- or lactate-grown cells. It is postulated that, in phosphate-deficient growth medium, gluconeogenic metabolism regulates alkaline phosphatase synthesis.
|
Interrelationship of carbohydrate metabolism and alkaline phosphatase synthesis in Bacillus licheniformis 749/c. Membrane-bound alkaline phosphatase of Bacillus licheniformis 749/c is derepressed by glucose in complex and chemically defined media. In the presence of lactate, pyruvate, or succinate the synthesis is repressed. The lactate repression neither affects total protein synthesis nor inhibits penicillinase synthesis. Thus, carbon sources specifically influence alkaline phosphatase synthesis. Although variations in the inorganic phosphate content of the growth media directly affect alkaline phosphatase synthesis, the intracellular inorganic and total phosphate pools appear to be unrelated to its repression or derepression. During lactate repression there is preferential incorporation of lactate molecules into glycogen, whereas no such incorporation could be detected from glucose. Net glycogen synthesis remains the same in glucose- or lactate-grown cells. It is postulated that, in phosphate-deficient growth medium, gluconeogenic metabolism regulates alkaline phosphatase synthesis.
|
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] |
PMID:19482
|
J. Edouard Samson Address: the autonomic nerve supply of bone. An experimental study of the intraosseous adrenergic nervi vasorum in the rabbit.
|
The anatomy of the autonomic sympathetic vasomotor nerve supply of bone was studied in rabbits by methods of histochemistry, and fluorescent and electron microscopy. Our observations show that the intraosseous vessels are richly supplied by adrenergic nerves. The large primary nerves are located on or about the surface of the vessel; the medium sized secondary nerves spiral around the long axis of vessels lying more deeply in the tunica adventitia; and the fine tertiary nerves form a rich plexus at the outer area of the tunica media. The tertiary nerves have various structures which probably contain neurotransmitter substance--that is, noradrenaline--and function as neuro-vasomuscular synapses. The sympathetic nerve supply of bone originates from the appropriate ganglion, and in the case of the tibial diaphysis it descends through the sciatic nerve and thereafter mainly through the medial popliteal nerve and enters the bone alongside the nutrient artery.
|
J. Edouard Samson Address: the autonomic nerve supply of bone. An experimental study of the intraosseous adrenergic nervi vasorum in the rabbit. The anatomy of the autonomic sympathetic vasomotor nerve supply of bone was studied in rabbits by methods of histochemistry, and fluorescent and electron microscopy. Our observations show that the intraosseous vessels are richly supplied by adrenergic nerves. The large primary nerves are located on or about the surface of the vessel; the medium sized secondary nerves spiral around the long axis of vessels lying more deeply in the tunica adventitia; and the fine tertiary nerves form a rich plexus at the outer area of the tunica media. The tertiary nerves have various structures which probably contain neurotransmitter substance--that is, noradrenaline--and function as neuro-vasomuscular synapses. The sympathetic nerve supply of bone originates from the appropriate ganglion, and in the case of the tibial diaphysis it descends through the sciatic nerve and thereafter mainly through the medial popliteal nerve and enters the bone alongside the nutrient artery.
|
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] |
PMID:19483
|
Coordinate control of collagen synthesis and cell growth in chick embryo fibroblasts and the effect of viral transformation on collagen synthesis.
|
Using collagenase digestion as an assay for collagen in partially synchronized secondary cultures of chick embryo fibroblasts, we find that the rate of collagen synthesis remains at a constant fraction of overall protein synthesis (5%) regardless of the growth rate of the cells even when the rate of protein synthesis is accelerated 5-fold by adding serum and altering the pH of the culture medium. However, in cells oncogenically transformed by Rous sarcoma virus, the relative rate of collagen synthesis was decreased by 50% 24 hours after infection and was 10% of the initial rate after 5 days. This selective decrease in rate of collagen synthesis could be reversed in cells infected with an RSV temperature-sensitive transformation-defective mutant at the non-permissive temperature, indicating that the decrease in the rate of collagen synthesis was not merely the result of viral infection but was a direct consequence of oncogenic transformation.
|
Coordinate control of collagen synthesis and cell growth in chick embryo fibroblasts and the effect of viral transformation on collagen synthesis. Using collagenase digestion as an assay for collagen in partially synchronized secondary cultures of chick embryo fibroblasts, we find that the rate of collagen synthesis remains at a constant fraction of overall protein synthesis (5%) regardless of the growth rate of the cells even when the rate of protein synthesis is accelerated 5-fold by adding serum and altering the pH of the culture medium. However, in cells oncogenically transformed by Rous sarcoma virus, the relative rate of collagen synthesis was decreased by 50% 24 hours after infection and was 10% of the initial rate after 5 days. This selective decrease in rate of collagen synthesis could be reversed in cells infected with an RSV temperature-sensitive transformation-defective mutant at the non-permissive temperature, indicating that the decrease in the rate of collagen synthesis was not merely the result of viral infection but was a direct consequence of oncogenic transformation.
|
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] |
PMID:19484
|
Effects of sugars on melanogenesis in cultured melanoma cells.
|
A permanent cell line C2M of mouse melanoma B16 was highly melanized in a modified Eagle's MEM supplemented with 10% calf serum, when the medium contained 1 mM galactose and 10 mM pyruvate instead of 5.5 mM glucose. The activity of the key anzyme for melanogenesis, tyrosinase (EC 1.14.18.1), of living cells cultured in the galactose-pyruvate medium was consistently 27 times higher than that of cells in normal MEM. This high level of tyrosinase activity was maintained in the stationary phase, in contrast to the activity of cells in normal medium, which decreased sharply in the stationary phase. It seems likely that tyrosinase activity is suppressed by the presence of glucose rather than stimulated by galactose. This modified medium should be useful obtaining a high level of tyrosinase activity in living cells in culture and in cell-free extracts.
|
Effects of sugars on melanogenesis in cultured melanoma cells. A permanent cell line C2M of mouse melanoma B16 was highly melanized in a modified Eagle's MEM supplemented with 10% calf serum, when the medium contained 1 mM galactose and 10 mM pyruvate instead of 5.5 mM glucose. The activity of the key anzyme for melanogenesis, tyrosinase (EC 1.14.18.1), of living cells cultured in the galactose-pyruvate medium was consistently 27 times higher than that of cells in normal MEM. This high level of tyrosinase activity was maintained in the stationary phase, in contrast to the activity of cells in normal medium, which decreased sharply in the stationary phase. It seems likely that tyrosinase activity is suppressed by the presence of glucose rather than stimulated by galactose. This modified medium should be useful obtaining a high level of tyrosinase activity in living cells in culture and in cell-free extracts.
|
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] |
PMID:19485
|
The self-assembly of synthetic filaments of myosin isolated from Chaos carolinensis and Amoeba proteus.
|
Synthetic myosin thick filaments were formed from preparations of electrophoretically homogeneous myosin isolated from Chaos carolinensis and Amoeba proteus when dialysed to physiological ionic strength and pH. Myosin dialysed directly against low ionic strength buffers formed native-like thick filaments in the presence and absence of exogenous divalent cations. The average dimensions of the synthetic filaments grown under these conditions were 455 nm long and 16 nm wide with a distinct bare central zone 174 nm long. Myosin predialysed against EGTA-EDTA solutions at high ionic strength and then dialysed to low ionic strength formed native-like filaments only in the presence of 1mM Mg2+. 1 mM Ca2+ could not be substituted for Mg2+ under these conditions to achieve native-like filaments. Filaments grown from predialysed myosin in the absence of Mg2+ resembled EGTA-dissociated myosin filaments observed in EGTA-treated cytoplasm and were highly branched, poorly formed filaments lacking a distinct bare central zone. The average dimensions of the filaments grown from predialysed myosin in the absence of Mg2+ were 328 nm long, 13 nm wide with a bare central zone 111 nm long. Under the conditions tested, myosin isolated from these amoebae did not demonstrate a divalent cation requirement for thick filament formation. The results obtained with myosin isolated from the 2 organisms were identical.
|
The self-assembly of synthetic filaments of myosin isolated from Chaos carolinensis and Amoeba proteus. Synthetic myosin thick filaments were formed from preparations of electrophoretically homogeneous myosin isolated from Chaos carolinensis and Amoeba proteus when dialysed to physiological ionic strength and pH. Myosin dialysed directly against low ionic strength buffers formed native-like thick filaments in the presence and absence of exogenous divalent cations. The average dimensions of the synthetic filaments grown under these conditions were 455 nm long and 16 nm wide with a distinct bare central zone 174 nm long. Myosin predialysed against EGTA-EDTA solutions at high ionic strength and then dialysed to low ionic strength formed native-like filaments only in the presence of 1mM Mg2+. 1 mM Ca2+ could not be substituted for Mg2+ under these conditions to achieve native-like filaments. Filaments grown from predialysed myosin in the absence of Mg2+ resembled EGTA-dissociated myosin filaments observed in EGTA-treated cytoplasm and were highly branched, poorly formed filaments lacking a distinct bare central zone. The average dimensions of the filaments grown from predialysed myosin in the absence of Mg2+ were 328 nm long, 13 nm wide with a bare central zone 111 nm long. Under the conditions tested, myosin isolated from these amoebae did not demonstrate a divalent cation requirement for thick filament formation. The results obtained with myosin isolated from the 2 organisms were identical.
|
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] |
PMID:19488
|
[Identification and quantitation of impurities from benorilate (Salipran) by high-performance liquid chromatography (author's transl)].
|
High-performance liquid chromatography is used for identification and quantitation of impurities which may be encountered in a new antalgic, benorilate (or Salipran), an ester of aspirin with paracetamol. Gradient elution is carried out using a stationary phase consisting of porous 10-micron silica beads bonded to alkylnitrile (Micropak CN), and a mixture of hexane-methylenechloride-methanol-acetic acid with varying methanol percentage as mobile phase. The following impurities were separated from benorilate: acetylsalicylic anhydride, aspirin, acetylsalicylsalicylic acid, salophene, amino-4-phenylacetoxy-2-benzoate, paracetamol, p-aminophenol. The repeatability of the quantitative analysis is good with a standard variation of 0.54% for benorilate (7 injections). Detection is by UV absorption at 254 nm, and detectability is between 2-10(-9) moles for p-aminophenol and 4-10(-11) moles for salophene.
|
[Identification and quantitation of impurities from benorilate (Salipran) by high-performance liquid chromatography (author's transl)]. High-performance liquid chromatography is used for identification and quantitation of impurities which may be encountered in a new antalgic, benorilate (or Salipran), an ester of aspirin with paracetamol. Gradient elution is carried out using a stationary phase consisting of porous 10-micron silica beads bonded to alkylnitrile (Micropak CN), and a mixture of hexane-methylenechloride-methanol-acetic acid with varying methanol percentage as mobile phase. The following impurities were separated from benorilate: acetylsalicylic anhydride, aspirin, acetylsalicylsalicylic acid, salophene, amino-4-phenylacetoxy-2-benzoate, paracetamol, p-aminophenol. The repeatability of the quantitative analysis is good with a standard variation of 0.54% for benorilate (7 injections). Detection is by UV absorption at 254 nm, and detectability is between 2-10(-9) moles for p-aminophenol and 4-10(-11) moles for salophene.
|
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] |
PMID:19490
|
Purification of alpha-L-fucosidase from various sources by affinity chromatography.
|
An affinity column for alpha-L-fucosidases was constructed by linking p-amino-phenyl 1-thio-alpha-L-fucopyranoside to Sepharose 4B through linkers of succinyl 3,3'-diamino-dipropylamine. Excellent purification of alpha-L-fucosidase from rat epididymis, Clostridium perfringens and Limulus polyphemus (horse shoecrab) could be effected inone step with good yield. An affinity column purification step can be introduced at any point in published purification procedures. The purified enzyme is essentially free of other glycosidases and proteolytic enzymes. The column material is stable and can be reused for at least two years.
|
Purification of alpha-L-fucosidase from various sources by affinity chromatography. An affinity column for alpha-L-fucosidases was constructed by linking p-amino-phenyl 1-thio-alpha-L-fucopyranoside to Sepharose 4B through linkers of succinyl 3,3'-diamino-dipropylamine. Excellent purification of alpha-L-fucosidase from rat epididymis, Clostridium perfringens and Limulus polyphemus (horse shoecrab) could be effected inone step with good yield. An affinity column purification step can be introduced at any point in published purification procedures. The purified enzyme is essentially free of other glycosidases and proteolytic enzymes. The column material is stable and can be reused for at least two years.
|
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] |
PMID:19492
|
Nickel gas chromatographic columns: an alternative to glass for biological samples.
|
Nickel tubing may be substituted for glass in the fabrication of gas chromatographic columns for use with samples of biological interest. Comparisons of separations of mixtures of steroids, narcotic alkaloids, phenothiazines, and amphetamines on stainless stell, glass, and nickel packed columns showed little or no observable sample decomposition on glass or nickel as contrasted to complete loss of certain compounds on stainless steel. The nickel columns are easily prepared, durable, economical, and not subject to breakage.
|
Nickel gas chromatographic columns: an alternative to glass for biological samples. Nickel tubing may be substituted for glass in the fabrication of gas chromatographic columns for use with samples of biological interest. Comparisons of separations of mixtures of steroids, narcotic alkaloids, phenothiazines, and amphetamines on stainless stell, glass, and nickel packed columns showed little or no observable sample decomposition on glass or nickel as contrasted to complete loss of certain compounds on stainless steel. The nickel columns are easily prepared, durable, economical, and not subject to breakage.
|
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] |
PMID:19495
|
Analysis of water soluble vitamins by high pressure liquid chromatography.
|
Resolution of the water-soluble vitamins--pyridoxin, riboflavin, niacinamide, vitamin B12, thiamin, ascorbic acid, niacin and folic acid--by high pressure liquid chromatography was examined on two bonded-phase columns, muBondapak C18 and muBondapak NH2. The effect on the retention times of individual vitamins and the separation of a multivitamin sample was determined using varying proportions of water/methanol as the eluting solvent and by addition of various salts, buffer solutions and PIC reagents to the water/methanol. Each vitamin was able to be eluted satisfactorily from muBondapak C18. It was found that seven vitamins could be resolved from a multivitamin mixture in a single analysis in several solvent systems with the total time for the analyses being always less than 40 min. With muBondapak NH2, all the vitamins except folic acid were eluted and six vitamins could be resolved from a mixture in a single analysis. The speed of analysis was greater with muBondapak NH2 with all compounds eluted in 15 min and the peaks were sharper. The order of elution was essentially the reverse of that obtained with muBondapak C18.
|
Analysis of water soluble vitamins by high pressure liquid chromatography. Resolution of the water-soluble vitamins--pyridoxin, riboflavin, niacinamide, vitamin B12, thiamin, ascorbic acid, niacin and folic acid--by high pressure liquid chromatography was examined on two bonded-phase columns, muBondapak C18 and muBondapak NH2. The effect on the retention times of individual vitamins and the separation of a multivitamin sample was determined using varying proportions of water/methanol as the eluting solvent and by addition of various salts, buffer solutions and PIC reagents to the water/methanol. Each vitamin was able to be eluted satisfactorily from muBondapak C18. It was found that seven vitamins could be resolved from a multivitamin mixture in a single analysis in several solvent systems with the total time for the analyses being always less than 40 min. With muBondapak NH2, all the vitamins except folic acid were eluted and six vitamins could be resolved from a mixture in a single analysis. The speed of analysis was greater with muBondapak NH2 with all compounds eluted in 15 min and the peaks were sharper. The order of elution was essentially the reverse of that obtained with muBondapak C18.
|
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] |
PMID:19496
|
Isolation of an obligately anaerobic Streptococcus pneumoniae from blood culture.
|
An obligately anaerobic strain of Streptococcus pneumoniae was isolated from blood culture in a 14-month-old child with an upper respiratory tract infection.
|
Isolation of an obligately anaerobic Streptococcus pneumoniae from blood culture. An obligately anaerobic strain of Streptococcus pneumoniae was isolated from blood culture in a 14-month-old child with an upper respiratory tract infection.
|
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] |
PMID:19497
|
Bicarbonate transport by rabbit cortical collecting tubules. Effect of acid and alkali loads in vivo on transport in vitro.
|
Rabbit cortical collecting tubules were perfused in vitro to investigate the control of bicarbonate transport. Bicarbonate was measured by microcalorimetry as total CO2. The perfusate and bath were identical solutions containing 25 mM bicarbonate at pH 7.4. The mean pH of the urine in the bladders of untreated rabbits at the time they were killed was 7.4. Their individual tubules, studied in vitro, either absorbed or secreted bicarbonate, and, combining the results, there was on the average no significant net transport. When the rabbits were treated with NH4Cl the day before the experiment, their urine was acidic and their tubules studied in vitro absorbed bicarbonate (i.e., there was net lumen-to-bath transport). In contrast, when the rabbits were treated with NaHCO3, their urine was significantly more alkaline, and their tubules studied in vitro generally secreted bicarbonate (i.e., net bath-to-lumen transport). Thus, the direction of bicarbonate transport by cortical collecting tubules studied under standard conditions in vitro correlated with the urine pH and was determined by the preceding treatment of the animals in vivo with acidifying or alkalinizing salts. These results demonstrate a previously unrecognized mechanism which contributes to the control of urinary bicarbonate excretion.
|
Bicarbonate transport by rabbit cortical collecting tubules. Effect of acid and alkali loads in vivo on transport in vitro. Rabbit cortical collecting tubules were perfused in vitro to investigate the control of bicarbonate transport. Bicarbonate was measured by microcalorimetry as total CO2. The perfusate and bath were identical solutions containing 25 mM bicarbonate at pH 7.4. The mean pH of the urine in the bladders of untreated rabbits at the time they were killed was 7.4. Their individual tubules, studied in vitro, either absorbed or secreted bicarbonate, and, combining the results, there was on the average no significant net transport. When the rabbits were treated with NH4Cl the day before the experiment, their urine was acidic and their tubules studied in vitro absorbed bicarbonate (i.e., there was net lumen-to-bath transport). In contrast, when the rabbits were treated with NaHCO3, their urine was significantly more alkaline, and their tubules studied in vitro generally secreted bicarbonate (i.e., net bath-to-lumen transport). Thus, the direction of bicarbonate transport by cortical collecting tubules studied under standard conditions in vitro correlated with the urine pH and was determined by the preceding treatment of the animals in vivo with acidifying or alkalinizing salts. These results demonstrate a previously unrecognized mechanism which contributes to the control of urinary bicarbonate excretion.
|
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] |
PMID:19498
|
Relationship between phosphaluria and acute hypercapnia in the rat.
|
Standard clearance studies were performed in mechanically ventilated intact and acutely thyroparathyroidectomized (TPTX) rats to document and characterize the effect of hypercapnia (HC) on urinary phosphorus excretion (U(P)V). HC as compared to normocapnia (NC) was associated with an increase in U(P)V in intact (62.5 vs. 7.93 mug/min) and TPTX (30.5 vs. 0.59 mug/min) rats, an increase in filtered load of phosphorus in intact (218 vs. 191 mug/min) and TPTX (243 vs. 146 mug/min) rats, an increase in blood bicarbonate concentration in intact (27.8 vs. 26.0 meq/liter) and TPTX (24.5 vs. 22.3 meq/liter) animals, and a decrease in blood pH in intact (7.15 vs. 7.42) and TPTX (7.07 vs. 7.39) rats. Additional TPTX rats with NC and HC were studied during phosphorus infusion at a comparable filtered load of phosphorus (NC = 307 mug/min and HC = 328 mug/min). U(P)V was 18.5 mug/min in NC and 85.2 mug/min in HC animals. Intact NC animals infused with NaHCO(3) achieved a blood bicarbonate of 45.9 meq/liter compared to 26.0 meq/liter in intact NC NaCl-infused rats. U(P)V was 10.0 mug/min in the NaHCO(3) and 7.93 mug/min in NaCl-infused animals. In intact HC animals infused with NaHCO(3), blood pH was 7.36 compared to 7.42 in NC intact NaCl-infused animals. U(P)V was 83.2 mug/min in the HC bicarbonate-infused and 7.93 mug/min in the NC NaCl-infused rats. These experiments demonstrate that elevated blood carbon dioxide tension per se increases U(P)V. Increases in filtered load of phosphorus and blood bicarbonate which are associated with HC contribute to the phosphaturia as does parathyroid hormone. The phosphaturia is not dependent upon reduction of extracellular pH.
|
Relationship between phosphaluria and acute hypercapnia in the rat. Standard clearance studies were performed in mechanically ventilated intact and acutely thyroparathyroidectomized (TPTX) rats to document and characterize the effect of hypercapnia (HC) on urinary phosphorus excretion (U(P)V). HC as compared to normocapnia (NC) was associated with an increase in U(P)V in intact (62.5 vs. 7.93 mug/min) and TPTX (30.5 vs. 0.59 mug/min) rats, an increase in filtered load of phosphorus in intact (218 vs. 191 mug/min) and TPTX (243 vs. 146 mug/min) rats, an increase in blood bicarbonate concentration in intact (27.8 vs. 26.0 meq/liter) and TPTX (24.5 vs. 22.3 meq/liter) animals, and a decrease in blood pH in intact (7.15 vs. 7.42) and TPTX (7.07 vs. 7.39) rats. Additional TPTX rats with NC and HC were studied during phosphorus infusion at a comparable filtered load of phosphorus (NC = 307 mug/min and HC = 328 mug/min). U(P)V was 18.5 mug/min in NC and 85.2 mug/min in HC animals. Intact NC animals infused with NaHCO(3) achieved a blood bicarbonate of 45.9 meq/liter compared to 26.0 meq/liter in intact NC NaCl-infused rats. U(P)V was 10.0 mug/min in the NaHCO(3) and 7.93 mug/min in NaCl-infused animals. In intact HC animals infused with NaHCO(3), blood pH was 7.36 compared to 7.42 in NC intact NaCl-infused animals. U(P)V was 83.2 mug/min in the HC bicarbonate-infused and 7.93 mug/min in the NC NaCl-infused rats. These experiments demonstrate that elevated blood carbon dioxide tension per se increases U(P)V. Increases in filtered load of phosphorus and blood bicarbonate which are associated with HC contribute to the phosphaturia as does parathyroid hormone. The phosphaturia is not dependent upon reduction of extracellular pH.
|
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] |
PMID:19499
|
Interactions among heparin, cold-insoluble globulin, and fibrinogen in formation of the heparin-precipitable fraction of plasma.
|
Fibrinogen and the cold-insoluble globulin of plasma (CIg) are the main protein components of the heparin-precipitable fraction of normal plasma. The interactions among these proteins and heparin were examined. Heparin formed a cold-precipitable complex with purified CIg or with mixtures of CIg and fibrinogen but not with purified fibrinogen alone. Cryoprecipitation was augmented by addition of Ca(++) or by selection of optimal heparin levels; it was reduced or even abolished by raising the ionic strength or pH or both, or by raising the heparin concentration above that for maximum precipitation of CIg. Fibrinogen reduced the threshold for heparin-induced CIg cryoprecipitation and, by coprecipitating with heparin and CIg, increased the amount of precipitate that formed. In contrast to the heparin-precipitable fraction of normal plasma which contained both fibrinogen and CIg, that from a patient with congenital afibrinogenemia contained CIg but lacked fibrinogen. Normal plasma depleted of CIg by immunoabsorption failed to form a heparin-induced cryoprecipitate. Thus, CIg is essential for heparin-induced cryoprecipitation to occur. Fibrinogen, as assessed by chromatographic experiments with heparin-Sepharose columns, had a considerably lower binding affinity for heparin than did CIg, suggesting that it participates in precipitate formation mainly, if not entirely, by virtue of its affinity for CIg. The region of the fibrinogen molecule accounting for its precipitation with CIg appears to be localized in the carboxy-terminal segment of the Aalpha-chain; fibrinogen subfractions lacking this region failed to augment cryoprecipitation of heparin-CIg mixtures and, even though such species were present in normal plasma, they failed to coprecipitate in the heparin-induced complex.
|
Interactions among heparin, cold-insoluble globulin, and fibrinogen in formation of the heparin-precipitable fraction of plasma. Fibrinogen and the cold-insoluble globulin of plasma (CIg) are the main protein components of the heparin-precipitable fraction of normal plasma. The interactions among these proteins and heparin were examined. Heparin formed a cold-precipitable complex with purified CIg or with mixtures of CIg and fibrinogen but not with purified fibrinogen alone. Cryoprecipitation was augmented by addition of Ca(++) or by selection of optimal heparin levels; it was reduced or even abolished by raising the ionic strength or pH or both, or by raising the heparin concentration above that for maximum precipitation of CIg. Fibrinogen reduced the threshold for heparin-induced CIg cryoprecipitation and, by coprecipitating with heparin and CIg, increased the amount of precipitate that formed. In contrast to the heparin-precipitable fraction of normal plasma which contained both fibrinogen and CIg, that from a patient with congenital afibrinogenemia contained CIg but lacked fibrinogen. Normal plasma depleted of CIg by immunoabsorption failed to form a heparin-induced cryoprecipitate. Thus, CIg is essential for heparin-induced cryoprecipitation to occur. Fibrinogen, as assessed by chromatographic experiments with heparin-Sepharose columns, had a considerably lower binding affinity for heparin than did CIg, suggesting that it participates in precipitate formation mainly, if not entirely, by virtue of its affinity for CIg. The region of the fibrinogen molecule accounting for its precipitation with CIg appears to be localized in the carboxy-terminal segment of the Aalpha-chain; fibrinogen subfractions lacking this region failed to augment cryoprecipitation of heparin-CIg mixtures and, even though such species were present in normal plasma, they failed to coprecipitate in the heparin-induced complex.
|
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] |
PMID:19500
|
Effects of hypermetabolism on ventilation and chemosensitivity.
|
Muscular exercise is associated with hypermetabolism and increased hypoxic ventilatory response (HVR). In order to dissociate mechanical and metabolic factors, the effect of hypermetabolism on hypoxic ventilatory response was evaluated at rest. Carbohydrate and protein feeding increases metabolic rate, and their effects on chemosensitivity, ventilation, and blood pH were evaluated in six normal subjects 2 h and 3 h after calorically equal test meals (1,000 cal). After carbohydrate, base-line oxygen consumption (Vo(2)) increased from 237+/-11.3 ml/min (SEM) to 302+/-19.4 (P < 0.001) and 303+/-18.5 (P < 0.001) at 2 h and 3 h, respectively. Hypoxic ventilatory response, measured as shape parameter A, increased from a control of 144+/-11.8 to 330+/-61.0 (P < 0.01) at 2 h and 286+/-57.0 (P < 0.05) at 3 h. These changes were associated with a mild metabolic acidosis as pH decreased from a control of 7.402+/-0.004 to 7.371+/-0.009 (P < 0.005) at 2 h and 7.377+/-0.008 (P < 0.005) at 3 h. After protein, Vo(2) increased from 241+/-6.7 to 265+/-6.2 (P < 0.02) and 270+/-5.4 (P < 0.001), an overall increase less than that which occurred after carbohydrate (P < 0.01). Hypoxic ventilatory response increased from 105+/-14.5 to 198+/-24.3 (P < 0.02) at 2 h and 219+/-17.3 (P < 0.01) at 3 h, which was not different from the increase with carbohydrate. After protein, no acidosis occurred. Thus, after protein, HVR increased despite the absence of a systemic acidosis. We conclude that both carbohydrate and protein feedings are associated with resting hypermetabolism and increased HVR compared with the fasting state. For both meals, increased metabolic rate was correlated with increased hypoxic response.
|
Effects of hypermetabolism on ventilation and chemosensitivity. Muscular exercise is associated with hypermetabolism and increased hypoxic ventilatory response (HVR). In order to dissociate mechanical and metabolic factors, the effect of hypermetabolism on hypoxic ventilatory response was evaluated at rest. Carbohydrate and protein feeding increases metabolic rate, and their effects on chemosensitivity, ventilation, and blood pH were evaluated in six normal subjects 2 h and 3 h after calorically equal test meals (1,000 cal). After carbohydrate, base-line oxygen consumption (Vo(2)) increased from 237+/-11.3 ml/min (SEM) to 302+/-19.4 (P < 0.001) and 303+/-18.5 (P < 0.001) at 2 h and 3 h, respectively. Hypoxic ventilatory response, measured as shape parameter A, increased from a control of 144+/-11.8 to 330+/-61.0 (P < 0.01) at 2 h and 286+/-57.0 (P < 0.05) at 3 h. These changes were associated with a mild metabolic acidosis as pH decreased from a control of 7.402+/-0.004 to 7.371+/-0.009 (P < 0.005) at 2 h and 7.377+/-0.008 (P < 0.005) at 3 h. After protein, Vo(2) increased from 241+/-6.7 to 265+/-6.2 (P < 0.02) and 270+/-5.4 (P < 0.001), an overall increase less than that which occurred after carbohydrate (P < 0.01). Hypoxic ventilatory response increased from 105+/-14.5 to 198+/-24.3 (P < 0.02) at 2 h and 219+/-17.3 (P < 0.01) at 3 h, which was not different from the increase with carbohydrate. After protein, no acidosis occurred. Thus, after protein, HVR increased despite the absence of a systemic acidosis. We conclude that both carbohydrate and protein feedings are associated with resting hypermetabolism and increased HVR compared with the fasting state. For both meals, increased metabolic rate was correlated with increased hypoxic response.
|
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] |
PMID:19501
|
The influence of thyroid hormones on in vitro erythropoiesis. Mediation by a receptor with beta adrenergic properties.
|
The erythropoietic effect of various thyroid hormones has been studied using erythroid colony formation by canine marrow cells. Although erythropoietin was required for colony growth, physiologic levels of thyroid hormones significantly enhanced colony numbers. The order of potency of the thyroid compounds in their in vitro erythropoietic effect parallels their known calorigenic potency in vivo, suggesting that the in vitro effect is physiologically relevant. A series of studies linked the mechanism of thyroid action to adrenergic receptors on responsive cells. Propranolol, a global beta-blocker, inhibited thyroid hormone-responsive erythroid colonies. When adrenergic antagonists having different blocking characteristics were added to culture, the thyroid hormone effect was blocked by those compounds having beta(2)-subspecificity. Velocity sedimentation analysis showed that the peak of colony-forming cells which respond to thyroid hormone and the adrenergic agonist, isoproterenol, sedimented at an identical rate (7.54 mm/h), which is slower than the major peak of colony-forming cells responding to erythropoietin alone (8.62 mm/h). These results demonstrate thyroid hormonal enhancement of in vitro erythroid colony growth which appears mediated by a receptor with beta(2)-adrenergic properties. The data suggest that changes in hormone-target cell interaction may occur during states of abnormal thyroid function.
|
The influence of thyroid hormones on in vitro erythropoiesis. Mediation by a receptor with beta adrenergic properties. The erythropoietic effect of various thyroid hormones has been studied using erythroid colony formation by canine marrow cells. Although erythropoietin was required for colony growth, physiologic levels of thyroid hormones significantly enhanced colony numbers. The order of potency of the thyroid compounds in their in vitro erythropoietic effect parallels their known calorigenic potency in vivo, suggesting that the in vitro effect is physiologically relevant. A series of studies linked the mechanism of thyroid action to adrenergic receptors on responsive cells. Propranolol, a global beta-blocker, inhibited thyroid hormone-responsive erythroid colonies. When adrenergic antagonists having different blocking characteristics were added to culture, the thyroid hormone effect was blocked by those compounds having beta(2)-subspecificity. Velocity sedimentation analysis showed that the peak of colony-forming cells which respond to thyroid hormone and the adrenergic agonist, isoproterenol, sedimented at an identical rate (7.54 mm/h), which is slower than the major peak of colony-forming cells responding to erythropoietin alone (8.62 mm/h). These results demonstrate thyroid hormonal enhancement of in vitro erythroid colony growth which appears mediated by a receptor with beta(2)-adrenergic properties. The data suggest that changes in hormone-target cell interaction may occur during states of abnormal thyroid function.
|
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] |
PMID:19502
|
Judgment of emotion among chronic schizophrenics.
|
This study investigated accuracy of judgment as to posed facial expressions and nonverbal scenes of various emotions. Ss were 16 male and 16 female chronic schizophrenics and a normal control group of equal size and sex composition. The results revealed that normal Ss were significantly more accurate than schizophrenics in identifying emotions from both posed photographs of the face and nonverbal videotape scenes. S sex was not found to affect differentially the schizophrenic or normal Ss' response accuracy to both the photographs and videotapes. Further, it was observed that both groups' accuracy improved when given multiple-choice alternatives to select from as contrasted to their open-ended free responses; this was especially true for the schizophrenic group. Teaching patients to identify and practice expressing discrete emotions was suggested.
|
Judgment of emotion among chronic schizophrenics. This study investigated accuracy of judgment as to posed facial expressions and nonverbal scenes of various emotions. Ss were 16 male and 16 female chronic schizophrenics and a normal control group of equal size and sex composition. The results revealed that normal Ss were significantly more accurate than schizophrenics in identifying emotions from both posed photographs of the face and nonverbal videotape scenes. S sex was not found to affect differentially the schizophrenic or normal Ss' response accuracy to both the photographs and videotapes. Further, it was observed that both groups' accuracy improved when given multiple-choice alternatives to select from as contrasted to their open-ended free responses; this was especially true for the schizophrenic group. Teaching patients to identify and practice expressing discrete emotions was suggested.
|
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] |
PMID:19503
|
The Brief Outpatient Psychopathology Scale (BOPS).
|
The pertinence of a rating scale capable of characterizing presenting psychopathology and measuring degrees of change for psychoneurotic patients treated in an outpatient setting is described. Data for 328 patients who represent 1191 rating profiles were used to develop the factor structure for the New Physician's Rating List, a rating scale completed by health professionals after Patient interviews. Findings were used to develop the new Brief Outpatient Psychopathology Scale. A proposed factor structure is discussed. The structures of both scales include an Anxiety Syndrome composed of Anxiety and Psychomotor Activation Factors. The scales also include Depression and Somatization factors.
|
The Brief Outpatient Psychopathology Scale (BOPS). The pertinence of a rating scale capable of characterizing presenting psychopathology and measuring degrees of change for psychoneurotic patients treated in an outpatient setting is described. Data for 328 patients who represent 1191 rating profiles were used to develop the factor structure for the New Physician's Rating List, a rating scale completed by health professionals after Patient interviews. Findings were used to develop the new Brief Outpatient Psychopathology Scale. A proposed factor structure is discussed. The structures of both scales include an Anxiety Syndrome composed of Anxiety and Psychomotor Activation Factors. The scales also include Depression and Somatization factors.
|
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] |
PMID:19504
|
Patients' expectancies and improvement in treatment: the shape of the link.
|
It has been hypothesized (a) that patients' expectancies for therapeutic gain are linked to the clinical improvement that the patients realize in treatment; and (b) that patients' expectancies may play a causative role in such improvement. The first hypothesis has received empirical support, but the second has not. This study tested the causativeinterpretation of patients' expectancies and a second interpretation, which states that patients' expectancies predict, but do not cause clinical improvement. The shape of thelink between expectancy and improvement for hospitalized schizophrenics was explored. Based on motivation research it was reasoned that a curvilinear relationship between expectancy and improvement would support a causative interpretation and that a linear relationship would support a predictive interpretation of the nature of expectancy. Multiple regression analyses found a linear relationship between expectancies and objective measures of improvement for the patients, but no evidence of a curvilinear relationship between these measures. The results were interpreted as supporting a predictive interpretation of the expectancies of hospitalized schizophrenic patients.
|
Patients' expectancies and improvement in treatment: the shape of the link. It has been hypothesized (a) that patients' expectancies for therapeutic gain are linked to the clinical improvement that the patients realize in treatment; and (b) that patients' expectancies may play a causative role in such improvement. The first hypothesis has received empirical support, but the second has not. This study tested the causativeinterpretation of patients' expectancies and a second interpretation, which states that patients' expectancies predict, but do not cause clinical improvement. The shape of thelink between expectancy and improvement for hospitalized schizophrenics was explored. Based on motivation research it was reasoned that a curvilinear relationship between expectancy and improvement would support a causative interpretation and that a linear relationship would support a predictive interpretation of the nature of expectancy. Multiple regression analyses found a linear relationship between expectancies and objective measures of improvement for the patients, but no evidence of a curvilinear relationship between these measures. The results were interpreted as supporting a predictive interpretation of the expectancies of hospitalized schizophrenic patients.
|
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] |
PMID:19505
|
Comparison of bumetanide and hydrochlorothiazide on renal potassium and hydrogen ion excretion.
|
The purpose of this study was to compare the renal electrolyte excretion pattern of bumetanide with that of hydrochlorothiazide in dogs anesthetized with pentobarbital. In bumetanide-treated animals, mean sodium excretion rose to 12 per cent of the filtered load, while hydrochlorothiazide increased sodium excretion to 4 per cent of the filtered load. After bumetanide, urine pH fell from 6.1 to 5.1 and net hydrogenion excretion increased significantly. After hydrochlorothiazide, urinary pH went from 6.4 to 7.4, and there was no change in net hydrogen ion excretion. Potassium excretion rose to 106+/-22 muEq/min with bumetanide and to 99+/-17 muEq/min with hydrochlorothiazide. These changes in electrolyte excretion occurred despite lack of changes in arterial blood gases, arterial blood pressure, and glomerular filtration rate. In addition, bumetanide did not exert an inhibitory effect on potassium excretion under conditions of potassium loading. It is concluded that bumetanide produces a higher urinary Na+:K+ ratio with a lower pH than hydrochlorothiazide and that renal potassium ion excretion in response to sulfamoyl diuretics is not solely dependent on the rate of sodium excretion.
|
Comparison of bumetanide and hydrochlorothiazide on renal potassium and hydrogen ion excretion. The purpose of this study was to compare the renal electrolyte excretion pattern of bumetanide with that of hydrochlorothiazide in dogs anesthetized with pentobarbital. In bumetanide-treated animals, mean sodium excretion rose to 12 per cent of the filtered load, while hydrochlorothiazide increased sodium excretion to 4 per cent of the filtered load. After bumetanide, urine pH fell from 6.1 to 5.1 and net hydrogenion excretion increased significantly. After hydrochlorothiazide, urinary pH went from 6.4 to 7.4, and there was no change in net hydrogen ion excretion. Potassium excretion rose to 106+/-22 muEq/min with bumetanide and to 99+/-17 muEq/min with hydrochlorothiazide. These changes in electrolyte excretion occurred despite lack of changes in arterial blood gases, arterial blood pressure, and glomerular filtration rate. In addition, bumetanide did not exert an inhibitory effect on potassium excretion under conditions of potassium loading. It is concluded that bumetanide produces a higher urinary Na+:K+ ratio with a lower pH than hydrochlorothiazide and that renal potassium ion excretion in response to sulfamoyl diuretics is not solely dependent on the rate of sodium excretion.
|
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] |
PMID:19507
|
Twin crossover relative potency analgesic assays in man. II. Morphine vs. 8-methoxycyclazocine.
|
Using the twin crossover, balanced incomplete block design described in the previous paper, a double-blind determination of the relative analgesic potency of graded intramuscular doses of Win 20,836 (8-methoxycyclazocine) and morphine was carried out in patients with postoperative pain. Although no preliminary data at all on the human analgesic activity of Win 20,836 were available, the sequential decision-making process designed to choose the doses of the test medication most closely equianalgesic with the standard functioned efficiently to establish doses of Win 20,836 that had analgesic activity. Unfortunately, the occurrence of psychotomimetic side effects prevented the administration of doses of Win 20,836 equieffective with the morphine standard, and this necessitated substantal extrapolation of the dose-response curve of the test drug to arrive at a relative potency estimate. However, our relative potency estimate, which indicated that Win 20,836 is three to six times as potent as morphine, was dependable enough to predict with reasonable certainty that doses of Win 20,836 equieffective to the usual doses of morphine would produce an unacceptable level of psychotomimetic side effects. Clinical investigation of the drug was therefore terminated.
|
Twin crossover relative potency analgesic assays in man. II. Morphine vs. 8-methoxycyclazocine. Using the twin crossover, balanced incomplete block design described in the previous paper, a double-blind determination of the relative analgesic potency of graded intramuscular doses of Win 20,836 (8-methoxycyclazocine) and morphine was carried out in patients with postoperative pain. Although no preliminary data at all on the human analgesic activity of Win 20,836 were available, the sequential decision-making process designed to choose the doses of the test medication most closely equianalgesic with the standard functioned efficiently to establish doses of Win 20,836 that had analgesic activity. Unfortunately, the occurrence of psychotomimetic side effects prevented the administration of doses of Win 20,836 equieffective with the morphine standard, and this necessitated substantal extrapolation of the dose-response curve of the test drug to arrive at a relative potency estimate. However, our relative potency estimate, which indicated that Win 20,836 is three to six times as potent as morphine, was dependable enough to predict with reasonable certainty that doses of Win 20,836 equieffective to the usual doses of morphine would produce an unacceptable level of psychotomimetic side effects. Clinical investigation of the drug was therefore terminated.
|
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] |
PMID:19511
|
Reactivity and aggression in the rat: induction by alpha-adrenergic blocking agents injected ventral to anterior septum but not into lateral septum.
|
Intracranial injections were made bilaterally through permanently implanted cannulas ending in the lateral septum or in the region ventral to the anterior septum. The rats were first screened with injections of a local anesthetic, lidocaine, which blocks both synaptic and axonal conduction. Those animals that showed an increase in reactivity and aggression were then injected with a synaptic transmitter blocking agent. The results showed that transmitter blocking agents reproduced the effect of the local anesthetic only in the region ventral to the anterior septum and that alpha-adrenergic (phentolamine, tolazoline), but not beta-adrenergic (propranolol, hydralazine), cholinergic (atropine, hyocine), or dopaminergic (haloperidol) blocking agents were effective. These results suggest that synapses in the forebrain system controlling reactivity and aggression are alpha-asrenergic and are located in the region ventral to the anterior septum just lateral to the diagonal band of Broca. The septum itself may be involved only to the extent that it is traversed by fibers of passage.
|
Reactivity and aggression in the rat: induction by alpha-adrenergic blocking agents injected ventral to anterior septum but not into lateral septum. Intracranial injections were made bilaterally through permanently implanted cannulas ending in the lateral septum or in the region ventral to the anterior septum. The rats were first screened with injections of a local anesthetic, lidocaine, which blocks both synaptic and axonal conduction. Those animals that showed an increase in reactivity and aggression were then injected with a synaptic transmitter blocking agent. The results showed that transmitter blocking agents reproduced the effect of the local anesthetic only in the region ventral to the anterior septum and that alpha-adrenergic (phentolamine, tolazoline), but not beta-adrenergic (propranolol, hydralazine), cholinergic (atropine, hyocine), or dopaminergic (haloperidol) blocking agents were effective. These results suggest that synapses in the forebrain system controlling reactivity and aggression are alpha-asrenergic and are located in the region ventral to the anterior septum just lateral to the diagonal band of Broca. The septum itself may be involved only to the extent that it is traversed by fibers of passage.
|
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] |
PMID:19508
|
Clinical pharmacokinetics of lorazepam. III. Intravenous injection. Preliminary results.
|
Four healthy male volunteers received 5 mg lorazepam as a single intravenous injection. Concentrations of lorazepam and its glucuronide metabolite were determined in multiple venous blood samples drawn during the 48 hours after dosing and in all urine collected during 96 hours after the dose. Mean pharmacokinetic parameters for lorazepam were: apparent elimination half-life, 13.2 hours; volume of distribution, 0.84 liter/kg; total clearance, 55.3 ml/min. Lorazepam glucuronide, the major metabolic product of lorazepam, promptly appeared in blood, reached peak levels within 6 hours of the dose, then declined in parallel with the parent compound. A mean of 69 per cent of the dose was recovered in urine as lorazepam glucuronide.
|
Clinical pharmacokinetics of lorazepam. III. Intravenous injection. Preliminary results. Four healthy male volunteers received 5 mg lorazepam as a single intravenous injection. Concentrations of lorazepam and its glucuronide metabolite were determined in multiple venous blood samples drawn during the 48 hours after dosing and in all urine collected during 96 hours after the dose. Mean pharmacokinetic parameters for lorazepam were: apparent elimination half-life, 13.2 hours; volume of distribution, 0.84 liter/kg; total clearance, 55.3 ml/min. Lorazepam glucuronide, the major metabolic product of lorazepam, promptly appeared in blood, reached peak levels within 6 hours of the dose, then declined in parallel with the parent compound. A mean of 69 per cent of the dose was recovered in urine as lorazepam glucuronide.
|
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] |
PMID:19506
|
Twin crossover relative potency analgesic assays in man. I. Morphine vs. morphine.
|
Although the four-point relative potency assay using crossover design has proven a powerful technique for the clinical evaluation of analgesics in patients with chronic pain, excessive dropouts have made this design impractical in postoperative pain. In a relative potency assay comparing single graded intramuscular doses of morphine standard and morphine test in postoperative patients, we have managed to circumvent this difficulty while preserving many of the advantages of a complete crossover by using the "twin-crossover" balanced incomplete block design, which requires that each subject receive only two of the four possible treatments. The "twin crossover" design, coupled with a sequential decision-making process that expedites choosing the doses of the test medication which are most closely equianalgesic with the standard, yielded excellent analgesic assay sensitivity and made efficient use of our population of postoperative patients.
|
Twin crossover relative potency analgesic assays in man. I. Morphine vs. morphine. Although the four-point relative potency assay using crossover design has proven a powerful technique for the clinical evaluation of analgesics in patients with chronic pain, excessive dropouts have made this design impractical in postoperative pain. In a relative potency assay comparing single graded intramuscular doses of morphine standard and morphine test in postoperative patients, we have managed to circumvent this difficulty while preserving many of the advantages of a complete crossover by using the "twin-crossover" balanced incomplete block design, which requires that each subject receive only two of the four possible treatments. The "twin crossover" design, coupled with a sequential decision-making process that expedites choosing the doses of the test medication which are most closely equianalgesic with the standard, yielded excellent analgesic assay sensitivity and made efficient use of our population of postoperative patients.
|
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] |
PMID:19510
|
Evaluation of butaclamol in chronic schizophrenic patients.
|
In a double-blind, placebo-controlled study, an attempt was made to evaluate butaclamol in chronic schizophrenic patients using chlorpromazine (CPZ) as the standard comparative drug. With doses up to 50 mg/day, butaclamol was shown to have significant antipsychotic activity comparable to CPZ but with a much higher incidence of extrapyramidal signs. A more reasonable maintenance dose may be in the range of 5 to 20 mg/day. Rebound insomnia was noted again with butaclamol, which warrants further study.
|
Evaluation of butaclamol in chronic schizophrenic patients. In a double-blind, placebo-controlled study, an attempt was made to evaluate butaclamol in chronic schizophrenic patients using chlorpromazine (CPZ) as the standard comparative drug. With doses up to 50 mg/day, butaclamol was shown to have significant antipsychotic activity comparable to CPZ but with a much higher incidence of extrapyramidal signs. A more reasonable maintenance dose may be in the range of 5 to 20 mg/day. Rebound insomnia was noted again with butaclamol, which warrants further study.
|
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0.03568178042769432,
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] |
PMID:19514
|
Metabolic and cardiovascular effects of carbuterol and metaproterenol.
|
Metabolic and cardiovascular responses to selective beta-adrenergic bronchodilators, carbuterol and metaproterenol, were studied during an asymptomatic period in 8 male subjects with bronchial asthma diagnosed as mile to moderate. On separate days each individual received either placebo, carbuterol 2 mg, carbuterol 4 mg, or metaproterenol 20 mg orally in a double-blind fashion. Subsequently, metabolic and cardiovascular responses were measured periodically for 5 hr. Carbuterol 2 mg was indistinguishable from placebo except for small elevations of glucose at 3 and 4 hr. Carbuterol 4 mg produced significant increases in glucose, insulin, lactate, and free fatty acids as well as in pulse rate and arterial pulse pressure. Metaproterenol produced increases only in plasma glucose and insulin. The majority of patients reported drug-related side effects which were all mild, after taking either carbuterol 4 mg or metaproterenol 20 mg. Fewer subjective side effects were noted with carbuterol 2 mg. These findings indicate that a 2-mg dose of carbuterol can be administered to typical asthmatic subjects without significant subjective or objective side effects. The larger dose (4 mg) may be accompanied by a greater frequency of side effects.
|
Metabolic and cardiovascular effects of carbuterol and metaproterenol. Metabolic and cardiovascular responses to selective beta-adrenergic bronchodilators, carbuterol and metaproterenol, were studied during an asymptomatic period in 8 male subjects with bronchial asthma diagnosed as mile to moderate. On separate days each individual received either placebo, carbuterol 2 mg, carbuterol 4 mg, or metaproterenol 20 mg orally in a double-blind fashion. Subsequently, metabolic and cardiovascular responses were measured periodically for 5 hr. Carbuterol 2 mg was indistinguishable from placebo except for small elevations of glucose at 3 and 4 hr. Carbuterol 4 mg produced significant increases in glucose, insulin, lactate, and free fatty acids as well as in pulse rate and arterial pulse pressure. Metaproterenol produced increases only in plasma glucose and insulin. The majority of patients reported drug-related side effects which were all mild, after taking either carbuterol 4 mg or metaproterenol 20 mg. Fewer subjective side effects were noted with carbuterol 2 mg. These findings indicate that a 2-mg dose of carbuterol can be administered to typical asthmatic subjects without significant subjective or objective side effects. The larger dose (4 mg) may be accompanied by a greater frequency of side effects.
|
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] |
PMID:19509
|
Clinical pharmacokinetics of lorazepam. IV. Long-term oral administration.
|
Fifteen healthy male volunteers received long-term daily treatment with oral lorazepam at doses as high as 10 mg per day for a period of 26 weeks. Steady-state plasma concentrations of lorazepam and its glucuronide metabolite were measured in all subjects at least every two weeks. At daily doses of 6 mg per day, the mean steady-state lorazepam level was 88 ng/ml and that of lorazepam glucuronide was 170 ng/ml. Mean levels among seven subjects who received 10 mg per day were 164 and 266 ng/ml, respectively. Lorazepam concentrations fluctuated from week to week despite constant dosage, but there was no evidence of systematic variation. Mean steady-state lorazepam levels were highly correlated with daily dose in mg/kg, but were not related to age. Lorazepam was not detected in any plasma samples drawn one week after discontinuation of treatment.
|
Clinical pharmacokinetics of lorazepam. IV. Long-term oral administration. Fifteen healthy male volunteers received long-term daily treatment with oral lorazepam at doses as high as 10 mg per day for a period of 26 weeks. Steady-state plasma concentrations of lorazepam and its glucuronide metabolite were measured in all subjects at least every two weeks. At daily doses of 6 mg per day, the mean steady-state lorazepam level was 88 ng/ml and that of lorazepam glucuronide was 170 ng/ml. Mean levels among seven subjects who received 10 mg per day were 164 and 266 ng/ml, respectively. Lorazepam concentrations fluctuated from week to week despite constant dosage, but there was no evidence of systematic variation. Mean steady-state lorazepam levels were highly correlated with daily dose in mg/kg, but were not related to age. Lorazepam was not detected in any plasma samples drawn one week after discontinuation of treatment.
|
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] |
PMID:19529
|
The dispersal of cells from human gynecologic specimens: chemical agents.
|
An investigation of nonenzymatic chemical solutions for the dispersal of gynecologic cells in suspension was undertaken using known general information on the composition of cell surfaces and cell adhesive properties. Studies on human cells cultured in vitro showed that thiol reducing agents release microextension-mediated contacts. Dispersing solutions containing lithium diiodosalicylate separated cells, presumably by extracting glycoproteins. Solutions without this agent but containing tetramethylurea and mixed sugars similar to those found on the cell surface separated cells by interacting with hydrogen bonds and other noncovalent polysaccharide interactions thought to hold cells together. Solutions containing ethylenediaminetetraacetate, dithiothreitol, tetramethylurea, mixed sugars, mixed amines and inorganic ions are suggested as mildly-acting dispersal solutions on the basis of evaluationtions by phase contrast microscopy, Papanicolaou staining and particle volume analysis.
|
The dispersal of cells from human gynecologic specimens: chemical agents. An investigation of nonenzymatic chemical solutions for the dispersal of gynecologic cells in suspension was undertaken using known general information on the composition of cell surfaces and cell adhesive properties. Studies on human cells cultured in vitro showed that thiol reducing agents release microextension-mediated contacts. Dispersing solutions containing lithium diiodosalicylate separated cells, presumably by extracting glycoproteins. Solutions without this agent but containing tetramethylurea and mixed sugars similar to those found on the cell surface separated cells by interacting with hydrogen bonds and other noncovalent polysaccharide interactions thought to hold cells together. Solutions containing ethylenediaminetetraacetate, dithiothreitol, tetramethylurea, mixed sugars, mixed amines and inorganic ions are suggested as mildly-acting dispersal solutions on the basis of evaluationtions by phase contrast microscopy, Papanicolaou staining and particle volume analysis.
|
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] |
PMID:19530
|
The antibody response to the T1699 murine adenocarcinoma: antibody class and subclass heterogeneity detected in serum and in situ.
|
We have used indirect immunofluorescence to study antibody responses directed against membrane antigens expressed on in vitro and in vivo T1699 mammary adenocarcinoma cells. IgG1, IgG2a, IgG2b, IgG3, IgA, and IgM antibodies were present in the serum of DBA/2 mice bearing T1699 tumors; IgG2a and IgG2b antibodies were readily detected on the cells in situ. Lesser amounts of the other classes and subclasses could be detected by indirect immunofluorescence measurements on in vivo tumor cells and with low pH eluates of in vivo cells tested on the in vitro line of T1699. The antigenic determinants on in situ tumor cells are not saturated with antibody as these cells demonstrated enhanced fluorescence of all immunoglobulin classes and subclasses when treated with autologous serum. Experiments with thymus-depleted mice indicated that immunoglobulin production was strongly dependent on thymus-derived cells for all immunoglobulin classes and subclasses except IgG2b. Our studies suggest that IgG2a may be active in the macrophage-mediated cytotoxic reaction and IgG2b in the immediate hypersensitivity reaction to T1699 cells. These results provide further evidence for an active role of tumor-specific antibody in the host defense to the T1699 adenocarcinoma in situ.
|
The antibody response to the T1699 murine adenocarcinoma: antibody class and subclass heterogeneity detected in serum and in situ. We have used indirect immunofluorescence to study antibody responses directed against membrane antigens expressed on in vitro and in vivo T1699 mammary adenocarcinoma cells. IgG1, IgG2a, IgG2b, IgG3, IgA, and IgM antibodies were present in the serum of DBA/2 mice bearing T1699 tumors; IgG2a and IgG2b antibodies were readily detected on the cells in situ. Lesser amounts of the other classes and subclasses could be detected by indirect immunofluorescence measurements on in vivo tumor cells and with low pH eluates of in vivo cells tested on the in vitro line of T1699. The antigenic determinants on in situ tumor cells are not saturated with antibody as these cells demonstrated enhanced fluorescence of all immunoglobulin classes and subclasses when treated with autologous serum. Experiments with thymus-depleted mice indicated that immunoglobulin production was strongly dependent on thymus-derived cells for all immunoglobulin classes and subclasses except IgG2b. Our studies suggest that IgG2a may be active in the macrophage-mediated cytotoxic reaction and IgG2b in the immediate hypersensitivity reaction to T1699 cells. These results provide further evidence for an active role of tumor-specific antibody in the host defense to the T1699 adenocarcinoma in situ.
|
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] |
PMID:19532
|
Sensitivity of amplifier T cells involved in the antibody response to type III pneumococcal polysaccharide to anti-lymphocyte serum.
|
Amplifier T cells responsible for enhancement of the antibody response to type III pneumococcal polysaccharide have been shown to be resistant to the effects of antilymphocyte serum (ALS) given at the time of immunization, a treatment that eliminates suppressor T cell activity. The resistance of amplifier T cells to ALS can be attributed to the fact that their activity develops after that of suppressor T cells. ALS given 1 or 2 days after immunization does abrogate amplifier T cell activity, independent of the mode by which that activity is elicited. The data emphasize the importance of kinetic considerations in understanding the effects produced by immunologically active agents such as ALS.
|
Sensitivity of amplifier T cells involved in the antibody response to type III pneumococcal polysaccharide to anti-lymphocyte serum. Amplifier T cells responsible for enhancement of the antibody response to type III pneumococcal polysaccharide have been shown to be resistant to the effects of antilymphocyte serum (ALS) given at the time of immunization, a treatment that eliminates suppressor T cell activity. The resistance of amplifier T cells to ALS can be attributed to the fact that their activity develops after that of suppressor T cells. ALS given 1 or 2 days after immunization does abrogate amplifier T cell activity, independent of the mode by which that activity is elicited. The data emphasize the importance of kinetic considerations in understanding the effects produced by immunologically active agents such as ALS.
|
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] |
PMID:19533
|
Effect of concanavalin A on lymphocyte interactions involved in the antibody response to type III pneumococcal polysaccharide. II. Ability of suppressor T cells to act on both B cells and amplified T cells to limit the magnitude of the antibody response.
|
When administered 2 days after immunization with 0.5 microgram Type III pneumococcal polysaccharide (SSS-III), the T lymphocyte mitogen concanavalin A (Con A) stimulates a 2.6-to 7-fold enhancement of the plaque-forming cells (PFC) response to SSS-III in vivo. This enhancement requires the presence of amplified T cells, which act by driving PFC or their precursors to extra rounds of proliferation. The extra proliferation that can be stimulated by Con A is not seen in the normal primary response to SSS-III; but treatment with anti-lymphocyte serum (ALS) to remove suppressor T cells will permit the additional proliferation to occur. This indicates that in the primary response to SSS-III, suppressor T cells act on amplifier T cells to limit the magnitude of the antibody response. Only suppression of B cells can account for the further suppression induced by Con A given at the time of immunization or by low-dose paralysis of the SSS-III response. The relatively late development of amplified activity compared to suppressor activity appears to account for the absence of amplifier activity after primary immunization with SSS-III. It is apparent that one can explain the regulatory effects observed during the development of an immune response to SSS-III only by considering both T cell- B cell and T cell- T cell interactions, together with the temporal relationships involved in those interactions.
|
Effect of concanavalin A on lymphocyte interactions involved in the antibody response to type III pneumococcal polysaccharide. II. Ability of suppressor T cells to act on both B cells and amplified T cells to limit the magnitude of the antibody response. When administered 2 days after immunization with 0.5 microgram Type III pneumococcal polysaccharide (SSS-III), the T lymphocyte mitogen concanavalin A (Con A) stimulates a 2.6-to 7-fold enhancement of the plaque-forming cells (PFC) response to SSS-III in vivo. This enhancement requires the presence of amplified T cells, which act by driving PFC or their precursors to extra rounds of proliferation. The extra proliferation that can be stimulated by Con A is not seen in the normal primary response to SSS-III; but treatment with anti-lymphocyte serum (ALS) to remove suppressor T cells will permit the additional proliferation to occur. This indicates that in the primary response to SSS-III, suppressor T cells act on amplifier T cells to limit the magnitude of the antibody response. Only suppression of B cells can account for the further suppression induced by Con A given at the time of immunization or by low-dose paralysis of the SSS-III response. The relatively late development of amplified activity compared to suppressor activity appears to account for the absence of amplifier activity after primary immunization with SSS-III. It is apparent that one can explain the regulatory effects observed during the development of an immune response to SSS-III only by considering both T cell- B cell and T cell- T cell interactions, together with the temporal relationships involved in those interactions.
|
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] |
PMID:19535
|
The presence of immunoregulatory cells in chicken thymus: function in B and T cell responses.
|
The presence of immunoregulatory cells in chicken thymus was studied by using several different systems. Chickens injected with large numbers of syngeneic thymocytes were tested for their ability to produce antibody to heterologous red cells. Similar chickens were studied for their ability to reject allogeneic skin grafts. In separate studies, mixtures of thymocytes with spleen cells or with peripheral blood leukocytes were assayed for their ability to respond to PHA or to produce a graft-vs-host reaction in embryonic chicks. These studies indicated that immunoregulatory cells exist in chicken thymus, which displays both helper and suppressor activity. The suppressor cells were more prevalent or more easily detectable in young birds and in chickens with intact bursas. The helper function of thymocytes was seen to better advantage with cells derived from older animals and from bursectomized donors.
|
The presence of immunoregulatory cells in chicken thymus: function in B and T cell responses. The presence of immunoregulatory cells in chicken thymus was studied by using several different systems. Chickens injected with large numbers of syngeneic thymocytes were tested for their ability to produce antibody to heterologous red cells. Similar chickens were studied for their ability to reject allogeneic skin grafts. In separate studies, mixtures of thymocytes with spleen cells or with peripheral blood leukocytes were assayed for their ability to respond to PHA or to produce a graft-vs-host reaction in embryonic chicks. These studies indicated that immunoregulatory cells exist in chicken thymus, which displays both helper and suppressor activity. The suppressor cells were more prevalent or more easily detectable in young birds and in chickens with intact bursas. The helper function of thymocytes was seen to better advantage with cells derived from older animals and from bursectomized donors.
|
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] |
PMID:19536
|
Immune responses during measles infection in immunosuppressed Rhesus monkeys.
|
Rhesus monkeys immunosuppressed with horse anti-human thymocyte gamma-globulin (ATG) were infected with measles and simultaneously inoculated with sheep erythrocytes (SRBC), a thymus-dependent antigen, and with pneumococcal polysaccaride type III (SSS-III), a thymus-independent antigen. ATG treatment alone suppressed SRBC antibody production, had no effect on SSS-III antibody production, and effectively eliminated circulating T cells compared to nonsuppressed monkeys. ATG treatment of measles-infected monkeys resulted in delayed virus clearance and delayed antibody production compared to nonsuppressed infected monkeys. After cessation of ATG treatment, measles antibodies and T cells reached normal levels, and measles virus was eliminated. Thus, immune clearance of measles virus is T cell-dependent, but the relative roles of cellular- and humoral-mediated immunity in vivo could not be clearly separated. Also, measles infection was associated with a decreased T cell mitogen responsiveness of circulating lymphocytes but not of lymph node lymphocytes, suggesting an altered circulating pattern of the cells responsible for delayed hypersensitivity. Also, measles infection had no effect on T-dependent antibody production to SRBC.
|
Immune responses during measles infection in immunosuppressed Rhesus monkeys. Rhesus monkeys immunosuppressed with horse anti-human thymocyte gamma-globulin (ATG) were infected with measles and simultaneously inoculated with sheep erythrocytes (SRBC), a thymus-dependent antigen, and with pneumococcal polysaccaride type III (SSS-III), a thymus-independent antigen. ATG treatment alone suppressed SRBC antibody production, had no effect on SSS-III antibody production, and effectively eliminated circulating T cells compared to nonsuppressed monkeys. ATG treatment of measles-infected monkeys resulted in delayed virus clearance and delayed antibody production compared to nonsuppressed infected monkeys. After cessation of ATG treatment, measles antibodies and T cells reached normal levels, and measles virus was eliminated. Thus, immune clearance of measles virus is T cell-dependent, but the relative roles of cellular- and humoral-mediated immunity in vivo could not be clearly separated. Also, measles infection was associated with a decreased T cell mitogen responsiveness of circulating lymphocytes but not of lymph node lymphocytes, suggesting an altered circulating pattern of the cells responsible for delayed hypersensitivity. Also, measles infection had no effect on T-dependent antibody production to SRBC.
|
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] |
PMID:19538
|
Cross-protective immunity to Gram-negative bacilli: studies with core glycolipid of Salmonella minnesota and antigens of Streptococcus pneumoniae.
|
Two immunoprophylactic approaches to the control of infections caused by gramnegative bacilli were evaluated by study of experimental infections in animals. The core glycolipid antigen derived from the Re mutant of Salmonella minnesota R595 is shared by virtually all enteric bacteria, and immunization with this endotoxin protects against the hemodynamic sequelae of bacterial infection and pyrexia without enhancing intravascular clearance of bacteria. The degree of protection afforded by active and passive immunization with core glycolipid was significantly less than that conferred by type-specific immunization. Escherichia coli and Klebsiella pneumoniae share capsular antigens with some strains of Streptococcus pneumoniae; by the mechanism of enhanced opsonization, antibodies to S. pneumoniae may cross-protect against infection with E. coli or K. pneumoniae.
|
Cross-protective immunity to Gram-negative bacilli: studies with core glycolipid of Salmonella minnesota and antigens of Streptococcus pneumoniae. Two immunoprophylactic approaches to the control of infections caused by gramnegative bacilli were evaluated by study of experimental infections in animals. The core glycolipid antigen derived from the Re mutant of Salmonella minnesota R595 is shared by virtually all enteric bacteria, and immunization with this endotoxin protects against the hemodynamic sequelae of bacterial infection and pyrexia without enhancing intravascular clearance of bacteria. The degree of protection afforded by active and passive immunization with core glycolipid was significantly less than that conferred by type-specific immunization. Escherichia coli and Klebsiella pneumoniae share capsular antigens with some strains of Streptococcus pneumoniae; by the mechanism of enhanced opsonization, antibodies to S. pneumoniae may cross-protect against infection with E. coli or K. pneumoniae.
|
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] |
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