ACTIVATION OF FIBROBLAST GROWTH-FACTOR (FGF) RECEPTORS BY RECOMBINANT HUMAN FGF-5

作者：CLEMENTS DA; WANG JK; DIONNE CA; GOLDFARB M

来源：Oncogene, 1993, 8(5): 1311-1316.

We have purified biologically active recombinant human fibroblast growth factor 5 (FGF-5) from Escherichia coli. In the presence of heparin, recombinant FGF-5 is as active as native growth factor, demonstrating that glycosylation does not significantly potentiate FGF-5 activity. FGF-5 can bind and induce autophosphorylation of human FGF receptors (FGFR) 1 and 2. Competition binding studies show that the K(D) for FGF-5-FGFR-1 and FGF-5-FGFR-2 interactions are both between 0.5 and 1.5 x 10(-9) M.

• 出版日期1993-5