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  • Title: [Catalytic activity of cytochrome P-448 in native and reconstituted microsomal membranes].
    Author: Grishanova AIu, Mishin VM, Liakhovich VV.
    Journal: Biokhimiia; 1984 Aug; 49(8):1343-9. PubMed ID: 6437454.
    Abstract:
    The dependence of oxidative activity of a microsomal monooxygenase system on the ratio of its constituent enzymes--cytochrome P-448 and NADPH-cytochrome P-450 reductase--was investigated. Two approaches for preparation of microsomal membranes with different contents of cytochrome P-448 were used, i. e., time-dependent induction by 3-methylcholanthrene and reconstitution of microsomal membranes by self-assembly from a mixture of solubilized microsomes of intact and methylcholanthrene-induced rats. Using antibodies against cytochrome P-448, the cytochrome P-448 content in native and reconstituted microsomal membranes and its participation in hydroxylation of benz(a)pyrene was determined. It was shown that benz(a)pyrene is hydroxylated in a membrane microsomal monooxygenase system more effectively, when the ratio of NADPH-cytochrome P-450 reductase to cytochrome P-448 is 1: 3 to 1: 6.
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