正常小鼠肝脏中表皮生长因子受体/蛋白激酶的纯化与特性分析

Cohen S, Fava R A, Sawyer S T

Proc Natl Acad Sci U S A. 1982 Oct;79(20):6237-41. doi: 10.1073/pnas.79.20.6237.

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.

我们通过亲和层析法从正常小鼠肝脏中纯化了表皮生长因子（EGF）受体/蛋白激酶。肝脏受体的生化特性与先前从人肿瘤细胞系A-431制备的EGF受体非常相似[科恩，S.，乌希罗，H.，斯托谢克，C. & 钦克斯，M.（1982年）《生物化学杂志》257，1523 - 1531]。肝脏中的EGF受体是一种分子量为170,000的糖蛋白。它能结合125I标记的EGF，并具有对酪氨酸残基具有特异性的EGF刺激的蛋白激酶活性。自身磷酸化和对外源底物的激酶活性均可得到证实。从正常小鼠肝脏中纯化的EGF受体与从人A-431细胞中纯化的受体在抗原性上相关。