Activation of fibroblast growth factor (FGF) receptors by recombinant human FGF-5
Clements, D.A.; Wang, J.K.; Dionne, C.A.; Goldfarb, M.
Oncogene 8(5): 1311-1316
1993
ISSN/ISBN: 0950-9232 PMID: 8386828 Document Number: 812
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 times 10-9 M.
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