[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.