[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.