Catalytic activity of the membrane‐bound methylcholanthrene‐inducible cytochrome P‐450

FEBS Letters

Lyakhovich, V.V.¹  Grishanova, A.Yu.¹  Mishin, V.M.¹ 

[1] Department of Cellular Physiology and Pathology, Institute of Clinical and Experimental Medicine, Academy of Medical Sciences of the USSR, Siberian Branch, 630091 Novosibirsk, USSR

关键词: Cytochrome P-450;    3-Methylcholanthrene;    3;    4-Benzopyrene;    NADPH-cytochrome P-450 reductase;    Cytochrome P-448 antibody;    MC;    methylcholanthrene;    BP;    benzopyrene;    PB;    phenobarbital;    3-OH BP;    3-hydroxybenzopyrene;   

DOI  :  10.1016/0014-5793(85)80194-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown