PMID: 43909Apr 1, 1979

The involvement of cytochrome P-488 and P-450 in NADH-dependent O-demethylation of p-nitroanisole in rat liver microsomes

Japanese Journal of Pharmacology
T KamatakiH Kitagawa


These studies have shown that addition of p-nitroanisole to a reaction mixture containing rat liver microsomes resulted in an increase the reoxidation rate of NADH-reduced cytochrome b5. Fortification of rat liver microsomes with partially purified cytochrome b5 produces an increase in both NADPH-dependent and NADH-dependent p-nitroanisole O-demethylation activity. Antiserum to cytochrome P-450 isolated from phenobarbital-treated rat liver microsomes inhibited the NADH-dependent O-demethylation activity as well as the NADPH-dependent O-demethylation activity seen in rat liver microsomes. Addition of either purified cytochrome P-450 or cytochrome P-448 to an incubation mixture containing phenobarbital-treated rat liver microsomes enhanced the NADH-dependent p-nitroanisole O-demethylation activity. These results suggest that NADH-dependent and, in part, NADPH-dependent O-demethylations are catalyzed by cytochrome P-448 and cytochrome P-450 receiving electrons from cytochrome b5.


Dec 1, 1993·Antimicrobial Agents and Chemotherapy·Y AokiM Arisawa
Nov 25, 1998·Comparative Biochemistry and Physiology. Part C, Pharmacology, Toxicology & Endocrinology·E TanakaT Horie
Apr 1, 1994·Xenobiotica; the Fate of Foreign Compounds in Biological Systems·E TanakaT Horie
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Related Concepts

Cytochrome P-450 Oxygenase
Respiratory Chain
Microsomes, Liver
Nitroanisole O-Demethylase

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