These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: [Immunochemistry of catalytic activity of cytochrome P-450-LM2 from rat liver microsomes].
    Author: Kurchenko VP, Usanov SA, Metelintsa DI.
    Journal: Biokhimiia; 1982 Sep; 47(9):1431-6. PubMed ID: 6814536.
    Abstract:
    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.
    [Abstract] [Full Text] [Related] [New Search]