Abstract
(1) Competition experiments have becn carried out with membrane-bound rat liver monoamine oxidase using tyramine, serotonin, dopamine, tryptamine, phenylethylamine, benzylamine and noradrenaline. Simple competitive kinetics were exhibited by most pairs of substrates. (2) Replots of the slopes of Lineweaver-Burk plots against inhibiting substrate concentration were linear in most cases but were hyperbolic for serotonin and α-methyl-tryptamine inhibition of tyramine and dopamine oxidation, and parabolic for noradrenaline and dopamine inhibition of tryptamine oxidation. (3) Simulation using an enzyme model having two independent catalytic sites was only partially successful in producing non-linear replots of the types obtained experimentally. (4) The nature of the catalytic sites of membrane-bound monoamine oxidase is discussed in the light of these results.
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