Abstract
Summary
An amine oxidase from rabbit aorta has been purified 20-fold. The enzyme possesses a substrate specificity pattern very similar to that found in rabbit plasma. The enzyme actively catalyzes the oxidation of alkylamines, benzylamine, tyramine, and tryptamine. The pH optimum with respect to benzylamine oxidation is pH 7.9. The enzyme is inhibited by a variety of agents which are known to attack carbonyl functions.
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