PT  - JOURNAL ARTICLE
AU  - EDWARD B. NELSON
AU  - P. PRITHVI RAJ
AU  - KENDRA J. BELFI
AU  - BETTIE SUE SILER MASTERS
TI  - OXIDATIVE DRUG METABOLISM IN HUMAN LIVER MICROSOMES
DP  - 1971 Sep 01
TA  - Journal of Pharmacology and Experimental Therapeutics
PG  - 580--588
VI  - 178
IP  - 3
4099  - http://jpet.aspetjournals.org/content/178/3/580.short
4100  - http://jpet.aspetjournals.org/content/178/3/580.full
SO  - J Pharmacol Exp Ther1971 Sep 01; 178
AB  - Isolated human liver microsomes were studied with respect to reduced nicotinamide adenine dinucleotide phosphate (NADPH)-cytochrome c reductase, NADPH-cytochrome P-450 reductase, aminopynine demethylase activity and the content of cytochrome P-450. Aminopyrine demethylation correlated well with the level of NADPH-cytochrome P-450 reductase activity and NADPH-cytochrome c reductase activity, but not with the content of cytochrome P-450. The mean values for cytochrome P-450 content and levels of both reductases were lower than those reported for laboratory animals. Antibodies prepared in rabbits to porcine liver NADPH-cytochrome c reductase concomitantly inhibited human NADPH-cytochrome c reductase, NADPH-cytochrome P-450 reductase and aminopyrine demethylation. Common precipitin lines were observed on Ouchterlony double diffusion plates between human and porcine liver microsomes. Thus, the flavoprotein involved in human liver microsomal drug metabolism is immunochemically and functionally similar to that of another mammalian species. © 1971 by The Williams & Wilkins Co.