[Reactivity of the LM4 form of cytochrome P-450 from rabbit liver microsomes].
Aniline oxidation and oxidative dimethylaniline demethylation with participation of the LM4 form of cytochrome P-450 from rabbit liver microsomes were studied under different conditions: e. g. after incorporation of LM4 form into microsomes of phenobarbital- and 3-methylcholanthrene-pretreated rabbits and after incorporation of this hemoprotein into liposomes in hydroperoxide-dependent reactions. The results obtained suggest that the LM4 form of cytochrome P-450 is catalytically inactive during aniline oxidation and dimethylaniline demethylation in both cases. The absence of catalytic activity of the LM4 form of cytochrome P-450 is due to the structural peculiarities of the active site of this hemoprotein rather than to its environment.
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D008748:Methylcholanthrene / Q000494:pharmacology; D008862:Microsomes, Liver / Q000187:drug effects / Q000378:metabolism*; D010634:Phenobarbital / Q000494:pharmacology; D011817:Rabbits
D008748:Methylcholanthrene; D003577:Cytochrome P-450 Enzyme System; D010634:Phenobarbital
Reaktsionnaia sposobnost' LM4-formy tsitokhroma P-450 iz mikrosom pecheni krolikov.