Purification of the epidermal growth factor receptor by tyrosine-Sepharose affinity chromatography |
| |
| Authors: | T Akiyama T Kadooka H Ogawara |
| |
| Affiliation: | 1. State Key Laboratory of Bioengineering Reactor, Shanghai Key Laboratory of New Drug Design, and School of Pharmacy, East China University of Science and Technology, 130 Mei-long Road, Shanghai 200237, China;2. Department of Pharmacology and Toxicology, and BIO5 Institute, University of Arizona, 1703 E. Mabel St., P. O. Box 210207, Tucson, AZ 85721-0207, USA;3. Corporate R&D Division, Firmenich Aromatics (China) Co., Ltd., Shanghai 201108, China |
| |
| 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. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
