منابع مشابه
NADPH: cytochrome P-450 reductase in olfactory epithelium. Relevance to cytochrome P-450-dependent reactions.
The presence of a very active cytochrome P-450-dependent drug-metabolizing system in the olfactory epithelium has been confirmed by using 7-ethoxycoumarin, 7-ethoxyresorufin, hexobarbitone and aniline as substrates, and the reasons for the marked activity of the cytochrome P-450 in this tissue have been investigated. The spectral interaction of hexobarbitone and aniline with hepatic and olfacto...
متن کاملRotation of cytochrome P-450. II. Specific interactions of cytochrome P-450 with NADPH-cytochrome P-450 reductase in phospholipid vesicles.
Purified rat liver microsomal cytochrome P-450 and NADPH-cytochrome P-450 reductase were co-reconstituted in phosphatidylcholine-phosphatidylethanolamine-phosphatidylserine vesicles using a cholate dialysis technique. The co-reconstitution of the enzymes was demonstrated in proteoliposomes fractionated by centrifugation in a glycerol gradient. The proteoliposomes catalyzed the N-demethylation o...
متن کاملCompetition between cytochrome P-450 isozymes for NADPH-cytochrome P-450 oxidoreductase affects drug metabolism.
NADPH-cytochrome P-450 oxidoreductase (CPR) is essential for the catalytic activity of cytochrome P-450 (P-450). On a molar basis, the amount of P-450 exceeds that of CPR in human liver. In this study, we investigated whether drug-drug interactions can occur as a result of competition between P-450 isozymes for this ancillary protein. For this purpose, combinations of P-450 isozymes were coexpr...
متن کاملNew developments in cytochrome P - 450 modeling
Presented here are the results of recent studies wfii-&-Gre designed to: ( 1 ) evaluate the role of the thiolate ligand, which is characteristic of P-450 structure, by incorporating it into model systems; ( 2 ) synthesize polypeptide-bound porphyrin to investigate the effects of heme environment on the activities; ( 3 ) apply appropriately designed P-450 mimics to drug metabolism studies and ev...
متن کاملCharacterization of a phenobarbital - inducible cytochrome P - 450 , NADPH - cytochrome P - 450 reductase and reconstituted cytochrome P - 450 mono - oxygenase system from rat brain
Cytochrome P-450 was purified to apparent homogeneity from the brain microsomes of phenobarbital-treated rats. The specific content of the purified P-450 was 12.7 nmol/mg of protein. NADPH-cytochrome P-450 reductase (reductase) was also purified to apparent homogeneity from brain microsomes. The specific content was 34.7,mol of cytochrome c reduced/min per mg of protein. The reduced carbon mono...
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ژورنال
عنوان ژورنال: Microbiology
سال: 1980
ISSN: 1350-0872,1465-2080
DOI: 10.1099/00221287-120-2-529