Purified EGF receptor–kinase interacts specifically with antibodies to Rous sarcoma virus transforming protein

Abstract

Transformation by several RNA tumour viruses seems to be mediated by virally coded protein kinases which specifically phosphorylate tyrosine^1–7. A tyrosine-specific protein kinase also seems to be involved in the mitogenic action of epidermal growth factor (EGF)⁸. This EGF-stimulated kinase activity is closely associated with the EGF receptor, with which it co-purifies during EGF-affinity chromatography⁹. Because both the virus- and EGF-stimulated tyrosine kinases may be involved in stimulation of cell growth, and because the viral kinases may be antigenically related to normal cell proteins^5,10–12, we examined the interaction of antibodies to viral tyrosine kinases with the affinity-purified EGF receptor–kinase preparation. We report here that the receptor–kinase specifically phosphorylates antibodies directed against the transforming protein kinase pp60^src of Rous sarcoma virus. However, none of these antibodies, including those which cross-react with the normal cellular homologue of pp60^src (pp60^sarc), precipitate the receptor–kinase. These results suggest that the EGF receptor–kinase is related to, but probably not identical with, pp60^sarc.