[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.