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A highly purified cytochrome P-450 from rabbit liver microsomes has been immobilized on albumin modified omega-aminohexyl-Sepharose 2B, after glutaraldehyde treatment of the matrix. The effect of the degree of albumin modification of the matrix on the catalytic activity of immobolized cytochrome P-450 has been studied in cumene hydroperoxide dependent aniline hydroxylation. On this basis an optimal cytochrome P-450/albumin ratio has been found which allows a substantial decrease in the rate of cytochrome P-450 destruction by cumene hydroperoxide in the substrate absence.
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