[Immunochemistry of catalytic activity of cytochrome P-450-LM2 from rat liver microsomes].
A systematic study of inhibition by antibodies of dimethylaniline (DMA) and aniline oxidation has been carried out under different conditions: e. g. with participation of intact, phenobarbital- and 3-methylcholantrene-induced microsomes, NADPH and O2; during hydroperoxide-dependent oxidation with three types of microsomes; in a reconstituted system containing cytochrome P-450 LM2, NADPH cytochrome P-450 reductase, NADPH and O2; in systems containing cytochrome P-450 LM2 and cumene hydroperoxide. In all cases the antibodies effectively inhibited oxidation of both substrates. The degree of inhibition increased in the following order: intact less than 3-methylcholantrene- less than phenobarbital-induced microsomes. In the case of hydroperoxide-dependent oxidation of aniline and DMA no complete inhibition was achieved.
D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex; D003577:Cytochrome P-450 Enzyme System / Q000276:immunology / Q000378:metabolism*; D005779:Immunodiffusion; D007700:Kinetics; D008748:Methylcholanthrene / Q000494:pharmacology; D008862:Microsomes, Liver / Q000187:drug effects / Q000201:enzymology*; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism; D010634:Phenobarbital / Q000494:pharmacology*; D011817:Rabbits
D000906:Antibodies; D000936:Antigen-Antibody Complex; D008748:Methylcholanthrene; D003577:Cytochrome P-450 Enzyme System; D009251:NADPH-Ferrihemoprotein Reductase; D010634:Phenobarbital
Immunokhimicheskoe izuchenie kataliticheskoĭ aktivnosti tsitokhroma P-450-LM2 iz mikrosom pecheni krolika.