[Immobilization of highly purified cytochrome P-450 from microsomes of rabbit liver].
Highly purified cytochrome P-450 from microsomes of the rabbit liver was immobilized on albumin modified Bio-gel P-300 using the glutaraldehyde method. The immobilized enzyme had a higher stability in storage and thermal stability than the soluble enzyme and retained catalytic activity toward cumene hydroperoxide-dependent aniline hydroxylation. Kinetic characteristics of cumene hydroperoxide-dependent aniline oxidation by solubilized and immobilized enzymes were compared.
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000302:isolation & purification / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D007700:Kinetics; D008862:Microsomes, Liver / Q000378:metabolism*; D011817:Rabbits; D013379:Substrate Specificity
D004800:Enzymes, Immobilized; D003577:Cytochrome P-450 Enzyme System
Immobilizatsiia vysokoochishchennogo tsitokhroma P-450 iz mikrosom pecheni krolika.