[Possible mechanism of the change in the catalytic properties of brain monoamine oxidase in rats].
An over two-fold decrease in the affinity of mitochondrial MAO to serotonin was found under hyperoxia, hypoxia and cold stress. At the same time serotonin deaminase and glucosamine deaminase activity was detected in the supernatant obtained after precipitation of the mitochondria. The data obtained indicate that the modification of the catalytic properties of MAO is caused both by alteration of the molecular properties of the enzyme and structural derangement of the mitochondrial membranes.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002384:Catalysis; D003080:Cold Temperature / Q000009:adverse effects; D003593:Cytoplasm / Q000201:enzymology; D003641:Deamination; D005260:Female; D000860:Hypoxia / Q000201:enzymology; D007700:Kinetics; D008297:Male; D008928:Mitochondria / Q000201:enzymology; D008995:Monoamine Oxidase / Q000378:metabolism*; D010100:Oxygen / Q000097:blood; D051381:Rats; D012701:Serotonin / Q000378:metabolism; D013312:Stress, Physiological / Q000201:enzymology
D012701:Serotonin; D008995:Monoamine Oxidase; D010100:Oxygen
Vozmozhnyĭ mekhanizm izmeneniia kataliticheskikh svoĭstv monoaminoksidazy mozga krys.