PURIFICATION OF THE EPIDERMAL GROWTH-FACTOR RECEPTOR BY TYROSINE-SEPHAROSE AFFINITY-CHROMATOGRAPHY

被引：52

作者：

AKIYAMA, T

KADOOKA, T

OGAWARA, H

机构：

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1985年 / 131卷 / 01期

关键词：

D O I：

10.1016/0006-291X(85)91822-4

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：

The EGF receptor has been purified from human epidermoid carcinoma A431 cells by affinity chromatography on wheat germ agglutinin-agarose and tyrosine-Sepharose. The purified EGF receptor was shown to be homogenous by SDS-polyacrylamide gel electrophoresis and possessed EGF-sensitive tyrosine kinase activity. Kinetic analysis of the autophosphorylation indicated that approximately 1.4 mol of phosphate was incorporated per mol of the EGF receptor. When a synthetic tyrosine-containing peptide was used as a phosphorylatable substrate, the specific activity of the EGF-stimulated kinase was 66 nmol/min/mg.

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页码：442 / 448

页数：7

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