Dimethylnitrosamine demethylation by reconstituted liver microsomal cytochrome P-450 enzyme system
نویسندگان
چکیده
منابع مشابه
Phospholipid requirement for dimethylnitrosamine demethylation by hamster hepatic microsomal cytochrome P-450 enzyme system.
Extraction with butan-1-ol of freeze-dried microsomal fractions from livers of 3-methyl-cholarthrene-pre-treated hamsters removed about 90% of the total lipid content, but the lipid remaining proved sufficient for the cytochrome P-450 enzyme system to retain about 15-40% of its original catalytic activity for dimethylnitrosamine demethylation. Addition of butan-1-ol-extracted total phospholipid...
متن کاملRole of phospholipid in electron transfer in a reconstituted liver microsomal enzyme system containing cytochrome P-450.
The enzyme system in liver microsomes which catalyzes the hydroxylation of fatty acids, hydrocarbons and a variety of drugs and other foreign compounds has been resolved into 3 components. These are: (a) a solubilized form of cytochrome P-450, (b) a solubilized form of NADPH-cytochrome P-450 reductase, and (c) a heat-stable component which has the solubility properties of a lipid. All 3 compone...
متن کاملRole 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...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1975
ISSN: 0264-6021
DOI: 10.1042/bj1520705