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. 1982 Oct;79(20):6237-41.
doi: 10.1073/pnas.79.20.6237.

Purification and characterization of epidermal growth factor receptor/protein kinase from normal mouse liver

S Cohen, R A Fava, S T Sawyer

Purification and characterization of epidermal growth factor receptor/protein kinase from normal mouse liver

S Cohen et al. Proc Natl Acad Sci U S A. 1982 Oct.

Abstract

We have purified the epidermal growth factor (EGF) receptor/protein kinase from the livers of normal mice by affinity chromatography. The biochemical properties of the liver receptor are very similar to those of the EGF receptor previously prepared from the human tumor cell line A-431 [Cohen, S., Ushiro, H., Stoscheck, C. & Chinkers, M. (1982) J. Biol. Chem. 257, 1523-1531]. The liver receptor for EGF is a glycoprotein of Mr 170,000. It binds 125I-labeled EGF and possesses an EGF-stimulable protein kinase activity specific for tyrosine residues. Both autophosphorylation and kinase activity toward exogenous substrates are demonstrable. The EGF receptor purified from normal mouse liver is antigenically related to the receptor purified from human A-431 cells.

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