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Title: Purification of the epidermal growth factor receptor by tyrosine-Sepharose affinity chromatography. Author: Akiyama T, Kadooka T, Ogawara H. Journal: Biochem Biophys Res Commun; 1985 Aug 30; 131(1):442-8. PubMed ID: 2994662. Abstract: 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 homogeneous 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.[Abstract] [Full Text] [Related] [New Search]