Liver microsomes from 3-methylcholanthrene-pretreated Long-Evans rats catalyzed the 2- and the 4-hydroxylation of biphenyl and the O-deethylation of ethoxyresorufin, sustained by either NADPH or cumene hydroperoxide. In contrast, the liver microsomes from corn oil- or phenobarbital-pretreated rats catalyzed the NADPH- or cumene hydroperoxide-sustained 4-hydroxylation of biphenyl, but the rates of 2-hydroxylation or ethoxyresorufin deethylation were negligible. A monooxygenase system reconstituted with partially purified NADPH-cytochrome c reductase and cytochrome P-448 catalyzed NADPH-supported biphenyl 2- and 4-hydroxylation and ethoxyresorufin deethylation. A monooxygenase system reconstituted with the reductase and cytochrome P-450 catalyzed NADPH-supported biphenyl 4-hydroxylation but exhibited negligible 2-hydroxylation or ethoxyresorufin deethylation activites. Solubilized cytochrome P-448 catalyzed biphenyl 2- and 4-hydroxylation and ethoxyresorufin deethylation sustained by cumene hydroperoxide in the absence of both NADPH and NADPH-cytochrome c reductase, whereas solubilized cytochrome P-450, under the same conditions, catalyzed only biphenyl 4-hydroxylation. It is concluded that the patterns of biphenyl hydroxylation and ethoxyresorufin deethylation observed with live- microsomes from untreated or inducer-treated rats are due largely to the inherent enzymic specificities of their cytochromes P-450 and P-448.

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nadphcytochrome c reductase monooxygenase enzymic specificities nadph 2 hydroperoxidesustained 4hydroxylation of biphenyl ethoxyresorufin deethylation cytochromes p450 and p448

M D, Burke R T, Mayer,.Inherent specificities of purified cytochromes P-450 and P-448 toward biphenyl hydroxylation and ethoxyresorufin deethylation.. 3 (4),245-53.

M D, Burke R T, Mayer,"Inherent specificities of purified cytochromes P-450 and P-448 toward biphenyl hydroxylation and ethoxyresorufin deethylation." 3

M D, Burke R T, Mayer,"Inherent specificities of purified cytochromes P-450 and P-448 toward biphenyl hydroxylation and ethoxyresorufin deethylation."