THE INVOLVEMENT OF CYTOCHROME P-448 AND P-450 IN NADH-DEPENDENT O-DEMETHYLATION OF p-NITROANISOLE IN RAT LIVER MICROSOMES
Open Access
- 1 January 1979
- journal article
- research article
- Published by Elsevier in The Japanese Journal of Pharmacology
- Vol. 29 (2) , 191-201
- https://doi.org/10.1254/jjp.29.191
Abstract
The addition of p-nitroanisole to a reaction mixture containing rat liver microsomes caused an increase in 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 and the NADPH-dependent O-demethylation activity seen in rat liver microsomes. Addition of 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. Apparently NADH-dependent and NADPH-dependent O-demethylations are catalyzed by cytochrome P-448 and cytochrome P-450 receiving electrons from cytochrome b5.This publication has 13 references indexed in Scilit:
- NADH-dependent O-demethylation of p-nitroanisole with rabbit liver microsomes.CHEMICAL & PHARMACEUTICAL BULLETIN, 1977
- NADH-dependent O-deethylation of p-nitrophenetole with rabbit liver microsomesArchives of Biochemistry and Biophysics, 1976
- Purification of a substrate complex of cytochrome P-450 from liver microsomes of 3-methylcholanthrene-treated rabbitsBiochemical and Biophysical Research Communications, 1976
- Specificity of antisera directed against rat liver cytochrome P-448Life Sciences, 1974
- A gel-electrophoretically homogeneous preparation of cytochrome P-450 from liver microsomes of phenobarbital-pretreated rabbitsBiochemical and Biophysical Research Communications, 1974
- Liver microsomal electron transport systems: II. The involvement of cytochrome b5 in the NADH-dependent hydroxylation of 3,4-benzpyrene by a reconstituted cytochrome P-448-containing systemBiochemical and Biophysical Research Communications, 1974
- Diphasic Binding of Carbon Monoxide with Cytochrome P-450 of Rat Liver Microsomes reduced by NADPHCHEMICAL & PHARMACEUTICAL BULLETIN, 1974
- Incorporation invitro of purified cytochrome b5 into liver microsomal membranesBiochemical and Biophysical Research Communications, 1973
- Reconstituted liver microsomal enzyme system that hydroxylates drugs, other foreign compounds and endogenous substratesArchives of Biochemistry and Biophysics, 1972
- Evidence for the participation of cytochrome b5 in hepatic microsomal mixed-function oxidation reactionsArchives of Biochemistry and Biophysics, 1971