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1.
Lab Delo ; (6): 20-4, 1991.
Article in Russian | MEDLINE | ID: mdl-1717744

ABSTRACT

Red cell aldehyde dehydrogenase (ALDH, EC 1.2.1.3) activity was measured by spectrophotometry in normal subjects and alcoholics after various periods of alcohol abstinence. ALDH was measured in all red cell hemolysate fractions; red cells were purified from hemoglobin by Sephadex CM-50 chromatography. The enzyme activity was found reduced in alcoholics' red cells as against that in controls. ALDH activities were somewhat increasing and approaching the normal values in the patients not using ethanol for 4 weeks or longer. These results recommend ALDH measurements in human red cells as a test for the detection of subjects abusing alcohol.


Subject(s)
Alcoholism/enzymology , Aldehyde Dehydrogenase/blood , Erythrocytes/enzymology , Adult , Alcoholism/blood , Humans , Male , Middle Aged
2.
Ukr Biokhim Zh (1978) ; 61(5): 29-34, 1989.
Article in Russian | MEDLINE | ID: mdl-2555950

ABSTRACT

Cholesterol was studied in experiments in vitro for its effect on the activity of Na, K-ATPase of the synaptic brain membranes of rats and a crystalline preparation of glutamate dehydrogenase from the liver mitochondria of a bull. Cholesterol decreased the activity of the above enzymes. When blocking guanidine groups of arginine residues of Na, K-ATPase and glutamate dehydrogenase the inhibiting action of cholesterol was absent. The obtained data evidence for the possibility of a direct interaction of cholesterol with membrane enzymes as well as for the important significance of guanidine groups of arginine residues of proteins in the process.


Subject(s)
Arginine/metabolism , Cholesterol/metabolism , Glutamate Dehydrogenase/metabolism , Guanidines/metabolism , Sodium-Potassium-Exchanging ATPase/metabolism , Animals , Brain/enzymology , Cattle , Guanidine , Male , Mitochondria, Liver/enzymology , Rats , Synaptic Membranes/enzymology
3.
Biull Eksp Biol Med ; 107(2): 196-9, 1989 Feb.
Article in Russian | MEDLINE | ID: mdl-2923976

ABSTRACT

The influence of intracisternal administration of antiserum to the neurospecific brain gamma gamma-enolase (aS-gamma gamma) on the consumption of 7.5% ethanol solution by rats was studied. Injection of aS-gamma gamma decreased the ethanol intake by the rats which had been drinking 15% solution of ethanol for 7 months as a single source of liquid. In vitro aS-gamma gamma caused 4-fold inhibition of the gamma gamma-enolase activity while it did not influence the alpha alpha-enolase activity. Intracisternal administration of aS-gamma gamma shifted enolase isoenzyme spectra in the direction of the decrease of gamma gamma-enolase content. It is suggested that the effect of aS-gamma gamma on ethanol consumption is due to inhibition of the activity of gamma gamma-enolase which participates in energy metabolism in neurons.


Subject(s)
Alcohol Drinking/drug effects , Brain/enzymology , Immune Sera/pharmacology , Phosphopyruvate Hydratase/immunology , Animals , Brain/immunology , Cisterna Magna , Drinking/drug effects , Immune Sera/administration & dosage , Immunization/methods , Phosphopyruvate Hydratase/analysis , Rabbits , Rats
4.
Farmakol Toksikol ; 47(6): 74-7, 1984.
Article in Russian | MEDLINE | ID: mdl-6519259

ABSTRACT

The binding of 14C-taurine by subcellular fractions of rat brain cortex was studied in vitro. The binding was discovered to be more marked in the presence of phenytoin. The stimulant effect of phenytoin was found to be dose-dependent. The other anticonvulsant drug phenobarbital was not shown to have any noticeable effect on 14C-taurine binding. Analogous results were obtained during investigation of 14C-taurine incorporation into cell cultures of neuroblastoma C1300.


Subject(s)
Anticonvulsants/pharmacology , Neurons/drug effects , Phenytoin/pharmacology , Taurine/metabolism , Animals , Brain/drug effects , Brain/metabolism , Cells, Cultured , Dose-Response Relationship, Drug , Neuroblastoma/metabolism , Neurons/metabolism , Phenobarbital/pharmacology , Rats , Stimulation, Chemical , Subcellular Fractions/drug effects , Subcellular Fractions/metabolism
5.
Fiziol Zh SSSR Im I M Sechenova ; 70(2): 125-9, 1984 Feb.
Article in Russian | MEDLINE | ID: mdl-6714462

ABSTRACT

Effects of ethimizole on the infraslow ascillations of the brain electrical activity were correlated with the pattern of its distribution within cellular structures. A negative wave of the infraslow activity was found to occur after the drug administration at the moment of its maximal inclusion into the two cellular fractions: the nuclei and the surface proteins of the endoplasmatic net. These structures seem to play part in changes of the central nervous system's functional state.


Subject(s)
Cerebral Cortex/physiology , Animals , Cerebral Cortex/drug effects , Cerebral Cortex/ultrastructure , Etimizol/metabolism , Etimizol/pharmacology , Male , Rats , Rats, Inbred Strains , Subcellular Fractions/metabolism , Time Factors
6.
Biull Eksp Biol Med ; 96(10): 53-5, 1983 Oct.
Article in Russian | MEDLINE | ID: mdl-6626731

ABSTRACT

The time course of 14C-etimizol distribution in cell structures of the rat cerebral cortex was studied. Two minutes after intraperitoneal injection etimizol penetrates brain cells. At this time the greater portion of the drug is found in cytosol. In five minutes the maximal part of the label gets bound with cell nuclei and microsomal protein fraction extracted with 0.14 M NaCl. These two cell fractions show the highest radioactivity throughout the entire observation period (up to 7 days). Since these fractions are reported to be capable of calcium accumulation, a suggestion is made that metabolic effects of etimizol are likely to be related to calcium metabolism.


Subject(s)
Cerebral Cortex/metabolism , Etimizol/metabolism , Imidazoles/metabolism , Animals , Carbon Radioisotopes , Cell Nucleus/metabolism , Etimizol/administration & dosage , Injections, Intraperitoneal , Male , Rats , Rats, Inbred Strains , Subcellular Fractions/metabolism , Time Factors
8.
Biokhimiia ; 41(11): 1952-7, 1976 Nov.
Article in Russian | MEDLINE | ID: mdl-14719

ABSTRACT

Ca2+ ions at low concentration (10(-4)-10(-5) M) when added to ultracentrifugates of sarcoplasmic proteins with minimal content of sarcoplasmic reticulum fragments completely prevent protein gelatinization or gels, formed in these conditions, quickly dilute. Ca2+ ions at the concentration of 10(-3) M prevented in these conditions gelatinization in all the cases studied. Strong gels of sarcoplasmic proteins are formed afterwards in weak acid (pH 6.1-6.75), neutral (pH 7.0) and weak alkaline (pH 7.25-7.45 and higher) media. It is suggested that gelatinization of sarcoplasmic proteins is closely related with the development of plastic tonus, obturatory muscle function and viscous after-effect.


Subject(s)
Muscle Proteins , Sarcoplasmic Reticulum , Animals , Calcium , Chemical Phenomena , Chemistry , Gels , Hydrogen-Ion Concentration , Muscles/physiology , Osmolar Concentration , Rabbits
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