作者: S. Cohen , H. Ushiro , C. Stoscheck , M. Chinkers
DOI: 10.1016/S0021-9258(19)68224-4
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摘要: A method is presented for the preparation of a "native" epidermal growth factor (EGF) receptor-kinase complex molecular weight 170,000 from A-431 cells. Although this receptor capable binding EGF, noncovalently, in quantities similar to previously isolated 150,000 (Cohen, S., Carpenter, G., and King, L., Jr. (1980) J. Biol. Chem. 255, 4834-4842), has 5 10 times intrinsic kinase activity (autophosphorylation). However, toward other proteins lower than that preparation. Both activities are enhanced by EGF. The also forming covalent linkages 125I-EGF, each precipitated antisera directed against protein. We suggest protein proteolytic degradation product EGF-enhanced remains associated with 125I-EGF-binding following EGF affinity chromatography, electrophoresis nondenaturing gels, or immunoprecipitation sodium dodecyl sulfate (SDS) gel-purified These results indicate receptor, kinase, substrate domains linked, possibly covalently.