Characterization of the interaction of 5'-p-fluorosulfonylbenzoyl adenosine with the epidermal growth factor receptor/protein kinase in A431 cell membranes.

摘要: Treatment of membrane vesicles from A431 cells, a human epidermoid carcinoma line, with the affinity label 5'-p-fluorosulfonylbenzoyl [8-14C]adenosine (5'-p-FSO2Bz[14C]Ado) results in an inhibition epidermal growth factor (EGF)-stimulable protein kinase and modification proteins having same molecular weight (Mr = 170,000 150,000) as receptor for EGF (Buhrow, S. A., Cohen, S., Staros, J. V. (1982) Biol. Chem. 257, 4019-4022). Modification 5'-p-FSO2BzAdo inhibits not only EGF-stimulated phosphorylation endogenous but also exogenous synthetic tyrosine-containing peptide substrate. This indicates that EGF-stimulable is modified by at site affecting catalytic activity. Membrane were treated 5'-p-FSO2Bz-[14C]Ado to kinase, then was purified chromatography on immobilized EGF. The thus contains 5'-p-SO2Bz[14C]Ado moiety. These data strongly support our hypothesis are two parts polypeptide chain.