[Immobilization of cytochrome P-450 from rabbit liver microsomes on albumin modified Sepharose 2B].
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.
D000418:Albumins; D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004355:Drug Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D007700:Kinetics; D008862:Microsomes, Liver / Q000378:metabolism*; D011817:Rabbits; D012685:Sepharose / Q000031:analogs & derivatives
D000418:Albumins; D004800:Enzymes, Immobilized; C024903:aminohexyl-sepharose; D012685:Sepharose; D003577:Cytochrome P-450 Enzyme System
Immobilizatsiia tsitokhroma P-450 iz mikrosom pecheni krolika na sefaroze-2B, modifitsirovannoĭ al'buminom.