Literature DB >> 6405660

A rapid one-step purification of NADPH-cytochrome c (P-450) reductase from rat liver microsomes.

E A Shephard, S F Pike, B R Rabin, I R Phillips.   

Abstract

NADPH-cytochrome c (P-450) reductase from liver microsomes of phenobarbital-treated rats has been purified in a single step by affinity chromatography on agarose-hexane-adenosine 2',5'-diphosphate. As determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, enzyme assay, and radioimmunoassay the protein obtained by this single step procedure is as pure as that isolated by multicolumn procedures.

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Year:  1983        PMID： 6405660     DOI： 10.1016/0003-2697(83)90573-0

Source DB:  PubMed          Journal:  Anal Biochem        ISSN： 0003-2697            Impact factor:   3.365


  2 in total

1.  Purification and characterization of the NADPH-cytochrome P-450 (cytochrome c) reductase from higher-plant microsomal fraction.

Authors:  I Benveniste; B Gabriac; F Durst
Journal:  Biochem J       Date:  1986-04-15       Impact factor: 3.857

2.  Species-specific differences and structure-activity relationships in the debromination of PBDE congeners in three fish species.

Authors:  Simon C Roberts; Pamela D Noyes; Evan P Gallagher; Heather M Stapleton
Journal:  Environ Sci Technol       Date:  2011-02-03       Impact factor: 9.028
  2 in total

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