Antibodies against a synthetic peptide as a probe for the kinase activity of the avian EGF receptor and v-erbB protein |
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Authors: | R M Kris I Lax W Gullick M D Waterfield A Ullrich M Fridkin J Schlessinger |
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Affiliation: | 1. Department of Chemical Immunology The Weizmann Institute of Science Rehovot 76100, Israel;2. Department of Chemistry The Weizmann Institute of Science Rehovot 76100, Israel;3. Imperial Cancer Research Fund Lincoln''s Inn Fields London WC2A 3PX, England;4. Department of Molecular Biology Genentech, Inc. 460 Point San Bruno Boulevard South San Francisco, California 94080 USA |
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Abstract: | The transforming protein v-erbB of avian erythroblastosis virus (AEV) displays extensive sequence homology with the presumptive protein-tyrosine kinase domain of the human EGF receptor and with the src protein-tyrosine kinase family of oncogenes. However, no kinase activity has previously been demonstrated for the v-erbB protein. Here antibodies generated against a synthetic peptide from the C terminus of human EGF receptor are shown to immunoprecipitate the EGF receptor from human and avian cells, as well as the v-erbB proteins from AEV-transformed cells that become phosphorylated on tyrosine residues upon the addition of gamma-32P-ATP. The immunoprecipitates are also able to phosphorylate exogenous tyrosine-containing substrates. Hence, it is likely that both avian EGF receptor and v-erbB proteins are protein tyrosine-specific protein kinases. Since the kinase activity of v-erbB protein cannot be regulated by EGF, it is proposed that the tyrosine protein kinase function of v-erbB may be constitutively activated. |
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