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Journal of Pharmacology And Experimental Therapeutics, Vol. 87, Issue 2, 149-158, 1946
Copyright © 1946 by American Society for Pharmacology and Experimental Therapeutics

STUDIES ON THE MECHANISM OF ACTION OF SYMPATHOMIMETIC AMINES

III. THE OXIDATION OF TYRAMINE BY RAT LIVER HOMOGENATES

WM. M. GOVIER 1, MARY E. GRELIS 1, NAOMI S. YANZ 1, and KARL H. BEYER 1

1 Department of Pharmacology, Medical Research Division, Sharp and Dohme, Inc., Glenolden, Pa.

The oxidation of tyramine by rat liver homogenates in vitro is stimulated by cytochrome C, coenzyme I, agr-keto acids, methylene blue, and aluminum and calcium ions. A possible mechanism of reaction involving a coupled reaction between a dehydrogenase ("amine oxidase") with tyramine as substrate and the lactic dehydrogenase in the presence of pyruvate, the cytochrome-cytochrome oxidase system serving as final path to oxygen, is described. This reaction is followed by oxidation of the p-hydroxyphenylacetaldehyde to p-hydroxyphenylacetic acid, possibly catalyzed by xanthine-aldehyde oxidase, Oxidation of the ring of tyramine also is suggested.

Submitted on April 2, 1946




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Copyright © 1946 by the American Society for Pharmacology and Experimental Therapeutics.