Properties of monoamine oxidase in monkey heart

Abstract

The activities of monoamine oxidase (MAO) in a homogenate and the mitochondrial fraction of monkey (Macaca fascicularis) heart were measured with labelled benzylamine, serotonin (5-HT), tyramine and beta-phenylethylamine (PEA) as substrates. The effects of clorgyline, deprenyl and semicarbazide on MAO were also investigated. Benzylamine deamination was more sensitive to deprenyl than to clorgyline, although it was not completely inhibited by a high concentration of either, and the remaining activity was completely inhibited by pretreatment with semicarbazide. The activities of 5-HT and tyramine were both more sensitive to clorgyline than to deprenyl, and both inhibitors gave single-sigmoidal inhibition curves. Experiments with increasing concentrations of PEA as substrate and clorgyline and deprenyl as inhibitors indicated that at higher concentrations, PEA was a substrate for MAO-A as well as MAO-B in monkey heart. These results suggest that monkey heart mitochondria contain not only MAO-A and MAO-B, but also clorgyline resistant amine oxidase (CRAO). The ratio of MAO-A, MAO-B and CRAO was determined from plots of inhibitions with each substrate. The kinetic constants of MAO in monkey heart were compared with those of MAO in hearts of other animals. The enzymic properties of MAO in monkey heart were discussed on the basis of these results.