The debrisoquine/sparteine-type polymorphism of drug oxidation presumably is caused by the absence or deficiency of cytochrome P-450 (P-450) isozyme(s). Using bufuralol 1‘-hydroxylation as a prototype reaction of this polymorphism, two functionally distinct forms, P-450 buf I and P-450 buf 11, with identical apparent M, of 50,000 were purified from liver microsomes of three different human live...

The 7a-hydroxylation of taurodeoxycholic acid and the 6&hydroxylation of taurochenodeoxycholic acid and lithocholic acid were studied with a reconstituted system from rat liver microsomes consisting of partially purified cytochrome P-450, NADPH-cytochrome P-450 reductase, a synthetic phosphatidylcholine and NADPH or an NADPH-generating system. 7a-Hydroxylase activity was observed with cytochrom...

Three forms of cytochrome P-450 were purified to homogeneity from liver microsomes of Wistar-strain rats treated with phenobarbital. They had minimum mol.wts. of 52 000, 53 000 and 54 000 as determined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and are designated as P-450(L), P-450(M) and P-450(H) respectively. They were shown to be immunoidentical by Ouchterlony double-diffu...

Cyclophosphamide was administered to adult male rats (130 mg/kg, single i.p. injection) and its effects on the P-450 enzymes that contribute to the activation of this drug in rat liver were then assessed. P-450-mediated cyclophosphamide 4-hydroxylase activity in isolated rat liver microsomes decreased by approximately 70% over a 9-day period following drug treatment. This decrease was due to th...

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