作者: Goldfarb M , Clements Da , Dionne Ca , Wang Jk
DOI:
关键词: Fibroblast growth factor-5 、 Biology 、 Growth factor 、 Fibroblast growth factor receptor 3 、 Biochemistry 、 Fibroblast growth factor 、 Fibroblast growth factor receptor 2 、 Fibroblast growth factor receptor 4 、 Growth factor receptor inhibitor 、 Cell biology 、 Fibroblast growth factor receptor
摘要: We have purified biologically active recombinant human fibroblast growth factor 5 (FGF-5) from Escherichia coli. In the presence of heparin, FGF-5 is as native factor, demonstrating that glycosylation does not significantly potentiate activity. can bind and induce autophosphorylation FGF receptors (FGFR) 1 2. Competition binding studies show KD for FGF-5-FGFR-1 FGF-5-FGFR-2 interactions are both between 0.5 1.5 x 10(-9) M.