The phenobarbital-type induction of rat liver microsomal monooxygenases by perfluorodecalin.

Induction of perfluorodecalin (PFD) of the liver microsomal system of metabolism of xenobiotics has been studied and compared with the inductions by phenobarbital (PB) and 3-methylcholanthrene (MC). It has been shown that PFD increases the content of cytochrome P-450, NADPH-cytochrome c reductase activity. Like PB, PFD induces the activities of benzphetamine-N-demethylase, aldrine-epoxidase, 16 beta-androstendion-hydroxylase.

Reappraisal of the liver benzpyrene hydroxylase synthesized de novo after treatment of rats with 2,3,7,8-tetrachlorodibenzo-p-dioxin and 3-methylcholanthrene.

The dynamics of the inductive effects of MC and TCDD upon rat liver microsomal benzpyrene hydroxylase and the main properties of the de novo synthesized hemoproteins have been compared. The inadequacy of expression of the enzyme activity per total cytochrome P-448 content has been established. It was concluded that TCDD microsomes have a relatively low content of benzpyrene hydroxylase with a higher molecular activity than the enzyme from MC microsomes.

Catalytic activity of the membrane-bound methylcholanthrene-inducible cytochrome P-450.

The benzopyrene hydroxylase activity of the methylcholanthrene-inducible form of cytochrome P-450 (P-448) has been studied in native and reconstituted liver microsomal membranes. The data obtained show that the molecular catalytic activity of membrane-bound cytochrome P-448 depends on the molar ratio of the cytochrome to NADPH-cytochrome P-450 reductase and that the optimal ratio for maximal activity of cytochrome P-448 in the microsomal membrane essentially differs from the equimolar one.