Diphasic Binding of Carbon Monoxide with Cytochrome P-450 of Rat Liver Microsomes reduced by NADPH
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منابع مشابه
Highly purified detergent-solubilized NADPH-cytochrome P-450 reductase from phenobarbital-induced rat liver microsomes.
NADPH-cytochrome P-450 reductase was highly purified from liver mlcrosomes of phenobarbital-induced rats by column chromatography on DEAE-cellulose, DEAE-Sephadex A-50, and hydroxylapatite in the presence of deoxycholate or Renex 690, a nonionic detergent. The purified enzyme gave a single major band with a molecular weight of 79,000 daltons on SDS-polyacrylamide gel electrophoresis. FFN and FA...
متن کاملProperties of NADPH-cytochrome P-450 reductase purified from rabbit liver microsomes.
NADPH-cytochrome P-450 reductase has been purified to electrophoretic homogeneity from rabbit liver microsomes by a procedure that may be used in conjunction with the isolation of the major forms of cytochrome P-450. The purified reductase is active in a reconstituted hydroxylation system containingp-45OLM, or P-~~OLM.,. The enzyme contains one molecule each of FMN and FAD per polypeptide chain...
متن کاملParticipation of cytochrome P-450 in reductive metabolism of 1-nitropyrene by rat liver microsomes.
Reductive metabolism of carcinogenic 1-nitropyrene by rat liver microsomes and reconstituted cytochrome P-450 systems was investigated. Under the nitrogen atmosphere, 1-aminopyrene was the only detected metabolite of 1-nitropyrene. The reductase activity in liver 105,000 X g supernatant fraction was ascribed to DT-diaphorase, aldehyde oxidase, and other unknown enzyme(s) from the results of cof...
متن کاملStudies on FAD- and FMN-binding domains in NADPH-cytochrome P-450 reductase from rabbit liver microsomes.
Six sulfhydryl group were determined after complete denaturation of NADPH-cytochrome P-450 reductase; of these, about 5.2 in both the native holoenzyme and FMN-depleted enzyme are accessible to p-hydroxychloromercuribenzoate (pCMB), which may be differentiated as follows: four --SH groups are modified by low concentration of the reagent but are not essentially involved in the catalytic function...
متن کاملExistence and separation of three forms of cytochrome P-450 from rat liver microsomes.
Rat liver microsomes contain three spectrally distinguishable forms of cytochrome P-450. Each form is identified qualitatively and quantitatively by visible spectral changes that occur when the cytochromes P-450 combine with various ligands, such as cyanide. In addition to cytochrome P-450, rat liver microsomes also contain cytochrome b6, which may be removed from the microsomes by digestion wi...
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ژورنال
عنوان ژورنال: Chemical and Pharmaceutical Bulletin
سال: 1974
ISSN: 0009-2363,1347-5223
DOI: 10.1248/cpb.22.171