PT  - JOURNAL ARTICLE
AU  - J C Kawalek
AU  - W Levin
AU  - D Ryan
AU  - A Y Lu
TI  - Reconstituted liver microsomal enzyme system that hydroxylates drugs, other foreign compounds, and endogenous substrates. IX. The formation of a 455-nm metabolite-cytochrome P-450 complex.
DP  - 1976 Mar 01
TA  - Drug Metabolism and Disposition
PG  - 190--194
VI  - 4
IP  - 2
4099  - http://dmd.aspetjournals.org/content/4/2/190.short
4100  - http://dmd.aspetjournals.org/content/4/2/190.full
SO  - Drug Metab Dispos1976 Mar 01; 4
AB  - The reconstituted liver microsomal hydroxylation system was used to study the formation of a metabolite-cytochrome P-450 complex absorbing maximally at 455 nm, with benzphetamine and N-hydroxyamphetamine as substrates. Complex formation required the presence of NADPH, substrate, NADPH-cytochrome c reductase, lipid, and cytochrome P-450, indicating that metabolism of the substrate is essential. In the presence of fixed amounts of lipid and NADPH-cytochrome c reductase, the rate of complex formation with cytochrome P-450 isolated from phenobarbital-treated rats was much greater than that observed with cytochrome P-48 from 3-methylcholanthrene-treated rats or rabbits. These results are consistent with recent studies indicating that different forms of cytochrome P-450 with distinct spectral, catalytic, and immunological properties exist in liver microsomes.