Abstract
Dealkylation activities of p-anisidine and p-phenetidine were increased by treatment of rats with either phenobarbital or 3-methylcholanthrene. Both substrates exhibited a type II difference spectrum when added to microsomes. NADPH-cytochrome P-450 reductase activity was inhibited by p-anisidine and p-phenetidine as well as by aniline. NADH-synergism was seen in the dealkylation of these substrates in hepatic microsomes from control, phenobarbital-treated, and 3-methylcholanthrene-treated rats. The addition of enhancers of aniline hydroxylation, 2,2′-bipyridine, and acetone resulted in an increased NADH-synergism of p-anisidine andp-phenetidine O-dealkylations. In the presence of these enhancers a slight NADH-synergism appeared even in aniline hydroxylation.
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