[Several kinetic features of membrane-dependent monoamine oxidase].
The v versus (S) plots for the initial rates of serotonin oxidation, catalyzed by monoamine oxidase in fragments of the rat liver or bovine brain mitochondrial membrane, had complicated non-hyperbolic shape, suggesting kinetic manifestation of cooperation in binding the substrate by the enzyme. A possibility of interactions of different monoamine oxidase types via the conformational alterations in the bio-membrane itself is considered.
D000818:Animals; D001921:Brain / Q000201:enzymology* / Q000648:ultrastructure; D002384:Catalysis; D002417:Cattle; D007700:Kinetics; D008297:Male; D008928:Mitochondria / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology*; D008956:Models, Chemical; D008995:Monoamine Oxidase / Q000378:metabolism*; D012701:Serotonin / Q000378:metabolism*
D012701:Serotonin; D008995:Monoamine Oxidase
Nekotorye kineticheskie osobennosti membranosviazannoĭ monoaminoksidazy