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2.
Article in Russian | MEDLINE | ID: mdl-6113723

ABSTRACT

In experiments on dogs with local neurosis-continuous flexion of the foreleg-changes were revealed in the beta-rhythm amplitude and the frequency of mean unit activity in the motor cortex, and the appearance and increased amplitude of the theta-rhythm in the hippocampus. Specific activity of Na+-K+-activated, and Mg2+-dependent ATPase decreases in subcortical fractions of the experimental animals' cerebral cortex by 55.0% in the synaptic membranes and 2 to 2.5 times in light and heavy synaptosomes, respectively. In similar fractions of the dorsal hippocampus, the activity of the enzyme decreases by 30.0% in the synaptic membranes and increases by 16.6% in the light synaptosomes and by 6.6% in the heavy ones.


Subject(s)
Adenosine Triphosphatases/metabolism , Hippocampus/ultrastructure , Motor Cortex/ultrastructure , Neurotic Disorders/pathology , Sodium-Potassium-Exchanging ATPase/metabolism , Animals , Ca(2+) Mg(2+)-ATPase , Dogs , Hippocampus/enzymology , Humans , Male , Microscopy, Electron , Motor Cortex/enzymology , Neural Analyzers/enzymology , Neural Analyzers/ultrastructure , Neurotic Disorders/enzymology
3.
Biokhimiia ; 45(10): 1829-32, 1980 Oct.
Article in Russian | MEDLINE | ID: mdl-7236770

ABSTRACT

The content of N-acetylneuraminic acid (ANA) was measured in the water-soluble and membrane fractions of the visual, locomotory, auditory and sensomotory divisions of rat brain cortex as well as in glycoproteins and glycolipids of the membrane fraction. The content of ANA in the water-soluble fraction of the visual, locomotory, auditory and sensomotory analyzers of brain cortex was 0.55, 0.56, 0.55 and 0.65 mkg/mg of dry weight, respectively. The ANA content in the membrane fraction was 9.2, 8.8, 8.2 and 8.4 mkg/mg of dry weight, respectively. The ANA content in the membrane fraction of glycoproteins was 2.8, 2.4, 2.2 and 2.8 mkg/mg of dry weight, respectively., that in the membrane fraction glycolipids--5.2, 7.2, 5.9 and 5.5 mkg/mg of dry weight, respectively. The ANA content in the membrane glycolipids of the locomotory division of rat brain cortex differed significantly from that of all the other divisions.


Subject(s)
Cerebral Cortex/analysis , Sialic Acids/analysis , Animals , Cell Membrane/analysis , Glycolipids/analysis , Glycoproteins/analysis , Membrane Lipids/analysis , Membrane Proteins/analysis , Motor Cortex/analysis , Rats , Solubility , Tissue Distribution , Visual Cortex/analysis
4.
Biokhimiia ; 45(5): 901-3, 1980 May.
Article in Russian | MEDLINE | ID: mdl-6246984

ABSTRACT

The specific activity of 5'-nucleotidase was measured in the fractions of myelin, synaptic membranes, heavy and light synaptosomes and purified mitochondria of brain cortex of intact rabbits. The enzyme specific activity in these fractions was practically the same and made up to 2.2, 2.1, 1.98 and 1.8 mkmoles of Pn per mg of protein per hr. The differences between the specific activities of the four fractions were statistically insignificant. The 5'-nucleotidase activity of the heavy synaptosome fraction was 2 times as low as that of the other fractions as was equal to 0.92 mkmoles of Pn per mg of protein per hr. This value is statistically different from those obtained during the analysis of the other fractions.


Subject(s)
Cerebral Cortex/enzymology , Nucleotidases/analysis , 5'-Nucleotidase , Animals , Kinetics , Rabbits , Subcellular Fractions/enzymology , Synaptosomes/enzymology
5.
Biokhimiia ; 44(8): 1502-5, 1979 Aug.
Article in Russian | MEDLINE | ID: mdl-497296

ABSTRACT

The total activity of aminoacyl-tRNA-synthetases of myelin, synaptic membranes, heavy and light synaptosomes, mitochondria and soluble fractions of rat cerebral cortex was studied. It was found that the highest activity of the enzymes is localized in the fractions of synaptic membranes and heavy and light synaptosomes and is practically absent in the myelin fraction. The specific activity of the total aminoacyl-tRNA-synthetase fraction in the soluble fraction is 2 times as low as compared to the synaptic membranes and light and heavy synaptosomes.


Subject(s)
Amino Acyl-tRNA Synthetases/metabolism , Cerebral Cortex/enzymology , Animals , Cytosol/enzymology , Male , Myelin Sheath/enzymology , Rats , Synaptic Membranes/enzymology , Synaptosomes/enzymology
6.
Biull Eksp Biol Med ; 85(3): 260-3, 1978 Mar.
Article in Russian | MEDLINE | ID: mdl-667316

ABSTRACT

Interrelationship between the motility of the small intestine and the intensity of energy formation in its smooth muscle layer was studied. The hexokinase activity was found to be significantly higher in the muscle layer of the duodenum as compared to that activity in the ileum and jejunum. No statistically significant differences in the hexokinase activity were revealed between the ileum and jejunum. The results obtained showed hexokinase activity to be highly variable, these values directly correlating with the motor activity of the intestinal muscle layer, representing the contractile apparatus of the intestine.


Subject(s)
Gastrointestinal Motility , Hexokinase/metabolism , Intestine, Small/physiology , Muscle, Smooth/enzymology , Animals , Cats , Duodenum/enzymology , Ileum/enzymology , Jejunum/enzymology , Male , Rats
7.
Tsitologiia ; 19(3): 384-7, 1977 Mar.
Article in Russian | MEDLINE | ID: mdl-883035

ABSTRACT

Crude mitochondrial fractions were fractionated into purified mitochondria, heavy- and light synaptosomes and synaptosomal membranes. The highest MAO activity was observed in purified mitochondria and heavy synaptosomes. Amphetamine strongly inhibited the MAO activity in heavy synaptosomes, and only slightly affected light synyptosomes. Electron microscopy of heavy synaptosomes revealed specific vesicles suggesting the presence of nerve endings of monoaminergic neurons, and the increase of the functional activity of these neurons.


Subject(s)
Amphetamine/pharmacology , Cerebral Cortex/drug effects , Monoamine Oxidase Inhibitors , Animals , Cerebral Cortex/enzymology , Cerebral Cortex/ultrastructure , Male , Mitochondria/enzymology , Rats , Synaptosomes/enzymology
8.
Biull Eksp Biol Med ; 81(2): 164-6, 1976 Feb.
Article in Russian | MEDLINE | ID: mdl-1276406

ABSTRACT

Neurospecific S-100 protein was revealed by the methods of microelectrophoresis in the 15% polyacrylamide gel with a 0.1% sodium dodecylsulfate and by a highly purified S-100 protein "marker" in the composition of low molecular acidic proteins of the rat brain synaptosomes. The S-100 protein conten constitutes about 15-2o% of the low molecular acidic synaptosomal porteins in the rat brain.


Subject(s)
Cerebral Cortex/ultrastructure , Nerve Tissue Proteins/analysis , S100 Proteins/analysis , Synaptosomes/analysis , Animals , Cerebral Cortex/analysis , Male , Rats
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