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Molecular Pharmacology, Vol 7, 301-307, Copyright © 1971 by the American Society for Pharmacology and Experimental Therapeutics

Mechanism of the Inhibition of Aldehyde Dehydrogenase in Vivo by Disulfiram and Diethyldithiocarbamate

RICHARD A. DEITRICH 1 and V. GENE ERWIN 1

1 Department of Pharmacology, University of Colorado School of Medicine, Denver, Colorado 80220, and School of Pharmacy, University of Colorado, Boulder, Colorado 80302

Aldehyde dehydrogenase in rat liver mitochondria and supernatant fluid has been assayed by following the rate of NADH production from NAD and aldehyde.

Although it is known that disulfiram is a much more potent inhibitor in vitro of aldehyde dehydrogenase than diethyldithiocarbamate, the administration of either compound to rats brings about a decrease in enzyme activity in the livers of such animals. Very similar dose-response curves are obtained if it is assumed that diethyldithiocarbamate undergoes reoxidation to disulfiram in vivo.

The decrease and return of activity of the supernatant and mitochondrial enzymes after disulfiram administration are identical in time course. The return of activity can be blocked by cycloheximide. These results indicate that disulfiram is an irreversible inhibitor of aldehyde dehydrogenase in vivo.

Note:
ACKNOWLEDGMENTS The excellent technical assistance of Mrs. Barbara Jensen and Miss Pequita Troxell is gratefully acknowledged.

Submitted on December 4, 1970




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