Inhibition of lipid peroxide decomposition by compounds which bind with cytochrome p-450.
The kinetics of lipid peroxide decomposition catalysed by microsomal enzymes and inhibited by SKF-525 A, hexobarbital, phenobarbital and aniline were investigated. The results indicate that the in vitro interaction of hexobarbital and SKF-525 A (type I binding compounds) with microsomal cytochrome p-450 inhibits the peroxidase activity while the in vitro interaction of aniline (type II binding compound) only slightly affect the peroxidase activity. It is suggested that LAHPO and type I binding compounds are competing for the hydrophobic binding site on cytochrome p-450, while type II binding compounds such as aniline negate electron transfer non-competitively by combining with the heme.
D000814:Aniline Compounds / Q000494:pharmacology; D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D006591:Hexobarbital / Q000494:pharmacology; D007700:Kinetics; D008054:Lipid Peroxides / Q000378:metabolism*; D008297:Male; D008862:Microsomes, Liver / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D010634:Phenobarbital / Q000494:pharmacology; D011335:Proadifen / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains
D000814:Aniline Compounds; D008054:Lipid Peroxides; D003577:Cytochrome P-450 Enzyme System; D011335:Proadifen; D006591:Hexobarbital; D010544:Peroxidases; C023650:aniline; D010634:Phenobarbital