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Molecular Pharmacology, Vol 7, 683-688, Copyright © 1971 by the American Society for Pharmacology and Experimental Therapeutics

Immunochemical Studies on the Role of Reduced Nicotinamide Adenine Dinucleotide Phosphate—Cytochrome c (P-450) Reductase in Drug Oxidation

ROBERT I. GLAZER 1, JOHN B. SCHENKMAN 1, and ALAN C. SARTORELLI 1

1 Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06510

Rabbit hyperimmune serum prepared to purified rat liver NADPH-cytochrome c rereductase (NADPH:cytochrome c oxidoreductase, EC 1.6.2.3) specifically inhibits the activity of this enzyme; thus, NADH-cytochrome c reductase was not affected. Measurement of the effects of the hyperimmune serum to NADPH-cytochrome c reductase on drug oxidation indicated that aminopyrine N-demethylation and aniline hydroxylation by rat liver microsomes from phenobarbital-treated animals, as well as benzpyrene hydroxylation by microsomes from 3-methylcholanthrene-treated animals, were inhibited. In addition, the activity of NADPH-cytochrome c reductase of normal, phenobarbital-treated, and 3-methylcholanthrene-treated rats was inhibited to the same extent by the ggr-globulin fraction prepared from hyperimmune serum. Liver NADPH cytochrome-P-450 reductase of animals treated with phenobarbital was also inhibited by the antireductase globulin. The results indicate that the NADPH-cytochrome P-450 reductases involved in drug oxidation by liver microsomes from normal, phenobarbital-treated, and 3-methylcholanthrene-treated animals are similar.

Submitted on April 13, 1971






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