Interactions of cytochrome P-450, NADPH-cytochrome P-450 reductase, phospholipid, and substrate in the reconstituted liver microsomal enzyme system.
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چکیده
منابع مشابه
Role of phospholipid in the reconstituted liver microsomal mixed function oxidase system containing cytochrome P-450 and NADPH-cytochrome P-450 reductase.
As described elsewhere (1-3), studies in this laboratory have led to the solubilization of liver microsomal cytochrome P-450 by treatment with deoxycholate and to its separation by ion exchange chromatography from NA DPH-cytochrome P450 reductase and a heat-stable lipid fraction. All three components are required, as well as mcilecular oxygen and NADPH, for the hydroxylation of drugs (4, 5), fa...
متن کاملPurified Liver Microsomal NADPH-Cytochrome P-450 Reductase
NADPH-cytochrome P-450 reductase was isolated from liver microsomes of phenobarbital-induced rats. The enzyme exhibits an apparent minimal molecular weight of 76,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and contains 1 molecule each of FMN and FAD. Trypsin treatment of the reductase yields an enzyme with an apparent minimal molecular weight of 69,000 which r...
متن کاملPurified Liver Microsomal NADPH-Cytochrome P-450 Reductase
NADPH-cytochrome P-450 reductase was isolated from liver microsomes of phenobarbital-induced rats. The enzyme exhibits an apparent minimal molecular weight of 76,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and contains 1 molecule each of FMN and FAD. Trypsin treatment of the reductase yields an enzyme with an apparent minimal molecular weight of 69,000 which r...
متن کاملInteraction of liver microsomal cytochrome P-450 and NADPH-cytochrome P-450 reductase in the presence and absence of lipid.
Phospholipid has been reported to be necessary for optimal catalytic activity of a number of mammalian cytochrome P-450 (P-450) systems. We also confirm that a number of individual phospholipids and mixtures, used as soluble monomers or phospholipid vesicles, show activation of 7-ethoxycoumarin O-deethylase activity by an enzyme system composed of rat liver microsomal P-450PB-B and NADPH-P-450 ...
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: Journal of Biological Chemistry
سال: 1980
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)85640-5