Activation of fibroblast growth factor (FGF) receptors by recombinant human FGF-5.

Published

Journal Article

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 KD for FGF-5-FGFR-1 and FGF-5-FGFR-2 interactions are both between 0.5 and 1.5 x 10(-9) M.

Full Text

Duke Authors

Cited Authors

  • Clements, DA; Wang, JK; Dionne, CA; Goldfarb, M

Published Date

  • May 1993

Published In

Volume / Issue

  • 8 / 5

Start / End Page

  • 1311 - 1316

PubMed ID

  • 8386828

Pubmed Central ID

  • 8386828

International Standard Serial Number (ISSN)

  • 0950-9232

Language

  • eng

Conference Location

  • England