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Molecular Pharmacology, Vol 11, 603-612, Copyright © 1975 by the American Society for Pharmacology and Experimental Therapeutics

Stable Enzyme Inhibitors and Stable Free Radical Species in Ultraviolet-Irradiated Solutions of Chlorpromazine

CHARLES GOUCHER 1, JOHN J. WINDLE 1, and LOUIS LEVY 1

1 Leprosy Research Unit, Public Health Service Hospital, San Francisco, California 94118, and United States Department of Agriculture Western Regional Research Laboratory, Albany, California 94710

Irradiated solutions of chlorpromazine inhibited the activities of yeast alcohol dehydrogenase (alcohol:NAD+ oxidoreductase, EC 1.1.1.1), beef heart lactate dehydrogenase (L-lactate:NAD+ oxidoreductase, EC 1.1.1.27), glyceraldehyde phosphate dehydrogenase [D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating), EC 1.2.1.12], and uridine diphosphoglucose dehydrogenase (uridine diphosphate glucose:NAD+ oxidoreductase, EC 1.1.1.22) even after long periods of storage in darkness at 40°. Two classes of products were obtained from irradiated chlorpromazine. Solutions of these products both inhibited enzyme activities and contained relatively stable free radicals. During and following free radical decay, the inhibitory activity of the solutions containing them was essentially unchanged. It is concluded that stable photolytic products in these solutions, other than free radicals, contributed predominantly to the inhibition of enzyme activity observed.

Submitted on January 8, 1975






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