[Interactions between the components of the cytochrome P-450-monoxygenase system from liver microsomes. III. N-demethylase activity of cytochrome P-450 relative to the degree of its integration].
Preceding experiments on the immobilization of the multi-component P-450 (LM) system, in which hte order of the first-immobilized component had been varied, gave evidence that the enzymatic activity depends on the degree of association. The present paper deals with the relationship between the degree of association and the demethylase activity. With rising concentrations of the detergent (Triton N-101) up to 0.2%, ultracentrifugation experiments have shown a steady decrease of the sedimentation coefficient from 20-22 down to 4.5 [S]. The demethylase activity (substrate benzphetamine) of the immobilized P-450 declines on reconstitution with solubilized reductase with raising degree of monomerization: 61% (0.02% Triton N-101) and 23% (0.2% Triton N-101) as compared with untreated fixed P-450 equals 100%. The demethylase activity can be increased by raising the reductase concentration in the test preparation.
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology*; D010088:Oxidoreductases / Q000378:metabolism; D010089:Oxidoreductases, N-Demethylating / Q000378:metabolism*; D011817:Rabbits
D003577:Cytochrome P-450 Enzyme System; D010088:Oxidoreductases; D010089:Oxidoreductases, N-Demethylating
Wechselwirkungen der Komponenten des Zytochrom P-450-Monooxygenasesystems aus Lebermikrosomen. III. Die N-Demethylaseaktivität von Zytochrom P-450 in Abhängigkeit vom Integrationsgrad.