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1 The Wellcome Research Laboratories, Burroughs Wellcome and Co., Inc. (U.S.A.), Tuckahoe, N. Y., and the Department of Pharmacology, Albert Einstein College of Medicine, New York, N. Y.
An enzyme system localized in liver microsomes which catalyzes the hydroxylation of tyramine to dopamine has been described. The rabbit possesses greater activity than the rat, guinea pig or mouse. Tyramine hydroxylase is inhibited in vitro by
-diethylaminoethyl diphenylpropyl acetate (SKF 525-A) , desmethylimipramine, N-o-chlorobenzyl-N , N"-dimethylguanidine (B.W. 392C60), and its dechloro analogue, bethanidine. In vivo studies show inhibition of this enzyme system by B.W. 392C60 and desmethylimipramine. It is of interest that B.W. 392C60 and bethanidine do not inhibit the in vitro oxidation of hexobarbital by liver microsomal enzymes.