[Interaction between cytochrome P-448 and NADP-cytochrome P-450 reductase in reconstituted microsomal membranes].
The regularities of changes in the functional activity of the microsomal monooxygenase system reconstituted by self-assembly from intact rat liver microsomes solubilized with 4% sodium cholate were studied at variable levels of NADPH-cytochrome P-450 reductase and the 3-methylcholanthrene-induced form of cytochrome P-450. Using antibodies against cytochrome P-448, the role of cytochrome P-448 in the overall reaction of benzopyrene hydroxylation induced in the microsomal membrane by a set of molecular forms of cytochrome P-450 was investigated. The effect of NADPH-cytochrome P-450 reductase and cytochrome P-448 incorporation into reconstituted microsomal membranes on benzpyrene metabolism suggests that in intact microsomal membranes benzopyrene metabolism induced by different forms of cytochrome P-450, with the exception of P-448, is limited by reductase is not the limiting component; however, cytochrome P-448 reveals its maximum activity at the cytochrome to reductase optimal molar ratio of 5:1; above this level, the catalytic activity of cytochrome P-448 is lowered.
D000818:Animals; D001579:Benzopyrene Hydroxylase / Q000378:metabolism; D002474:Cell-Free System; D019388:Cytochrome P-450 CYP1A2; D003579:Cytochrome Reductases / Q000378:metabolism*; D003580:Cytochromes / Q000378:metabolism*; D004790:Enzyme Induction; D007700:Kinetics; D008748:Methylcholanthrene / Q000494:pharmacology; D008862:Microsomes, Liver / Q000201:enzymology*; D009245:NADH Dehydrogenase / Q000378:metabolism*; D051381:Rats
D003580:Cytochromes; D008748:Methylcholanthrene; D001579:Benzopyrene Hydroxylase; C017170:Cyp1a2 protein, rat; D019388:Cytochrome P-450 CYP1A2; D003579:Cytochrome Reductases; D009245:NADH Dehydrogenase
Vzaimodoĭstvie tsitokhroma P-448 i NADPH-tsitokhrom P-450-reduktazy v rekonstruirovannykh mikrosomnykh membranakh.