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| Oncogene May (1993); 8(5):1311-6 | |
| Activation of fibroblast growth factor (FGF) receptors by recombinant human FGF-5. | |
| Clements DA, Wang JK, Dionne CA, Goldfarb M | |
| Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, New York, New York 10032. | |
| Abstract: 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. | |
| [PUBMED: 8386828] |   |
| Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |