ARTIFACTS IN ISOELECTRIC-FOCUSING OF THE MICROSOMAL-ENZYMES CYTOCHROME-P-450 AND NADPH-CYTOCHROME-P-450 REDUCTASE

被引：21

作者：

GUENGERICH, FP ^{[1
]}

机构：

[1] VANDERBILT UNIV,SCH MED,CTR ENVIRONM TOXICOL,NASHVILLE,TN 37232

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 577卷 / 01期

关键词：

(Liver microsome); Cytochrome P-450 reductase; Isoelectric focusing; NADPH-cytochrome P-450 reductase;

D O I：

10.1016/0005-2795(79)90015-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Highly-purified rat liver microsomal cytochrome P-450 and NADPH-cytochrome P-450 reductase (NADPH-ferricytochrome oxidoreductase, EC 1.6.2.4) preparations gave rise to a large number of bands under a variety of isoelectric focusing conditions, as observed after staining for either zymogen or protein. The binding patterns were not independent of sample concentration and position of application, and eluted bands did not refocus as expected. The artifactual heterogeneity is attributed to strong protein-protein interactions and perhaps to complexation of proteins with carrier ampholytes. These findings suggest caution in using isoelectric focusing to resolve mixtures of membrane proteins. © 1979.

引用

页码：132 / 141

页数：10

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