Studies on the localization of oxidative phosphorylation in cytoplasmic structures of rat liver.
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Animals↗
Biomedical subjects
L Venkov
Publications and source records attributed to L Venkov.
[Differences in the enzymatic activity of mitochondria from enriched neuronal and glial fractions].
Studies were performed in the activities of certain enzymes from oxidoreductase group: cytochrome c-oxidoreductase (EC 1.6.99.3), succinate dehydrogenase succinates: cytochrome c-oxidoreductase (EC 1.3.99.1), cytochrome oxidase (EC 1.9.3.1) and malate dehydrogenase (EC 1.1.1.37) in mitochondria from neuronal and glial-enriched fractions. The mitochondrial fraction purity was observed by the electron microscope. The enzyme activity of the glial mitochondrial fraction was much higher than that in the neuronal mitochondria. Malate dehydrogenase from glial enriched fraction consists of three isoenzymes, while neuronal mitochondria had two isoenzymes of malate dehydrogenase. The neuronal mitochondria were found to be more stable to lubrol and digitonin.
Animals↗
[Effect of motor regimes on water-soluble and membrane proteins and cholinesterase activity in subcellular fractions of rat brain tissue].
Albino rats were kept for a year under conditions of everyday motor loading or of a constant hypokinesia. An increase of the motor activity results in rise in the acetylcholinesterase activity determined in the synaptosomal and purified mitochondrial fractions while hypokinesia induces a pronounced decrease in this enzyme activity. The butyrylcholinesterase activity somewhat decreases in the synaptosomal fraction after hypokinesa but does not change under the motor loading regime. Motor loading causes an increase in the amount of synaptosomal water-soluble proteins possessing an intermediate electrophoretic mobility and seem to correspond to the brain-specific protein 14-3-2. In the synaptosomal fraction the amount of membrane proteins with a low electrophoretic mobility and with the cholinesterase activity rises. Hypokinesia, on the contrary, decreases the amount of these membrane proteins.
Acetylcholinesterase↗