RT Journal Article
SR Electronic
T1 Immunochemical Studies on the Role of Reduced Nicotinamide Adenine Dinucleotide Phosphate—Cytochrome c (P-450) Reductase in Drug Oxidation
JF Molecular Pharmacology
JO Mol Pharmacol
FD American Society for Pharmacology and Experimental Therapeutics
SP 683
OP 688
VO 7
IS 6
A1 GLAZER, ROBERT I.
A1 SCHENKMAN, JOHN B.
A1 SARTORELLI, ALAN C.
YR 1971
UL http://molpharm.aspetjournals.org/content/7/6/683.abstract
AB 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 γ-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.