Abstract : Acidic and basic fibroblast growth factors (FGFs) influence cell division and differentiation in retina cells. Their effects are thought to be mainly mediated through stimulation of a specific membrane receptor and subsequent generation of an intracellular signal pathway. In this study, we purified a FGF receptor of 130 kDa from bovine neural retina using wheat germ agglutinin affinity chromatography followed by FGF-affinity chromatography. The isolated receptor showed ligand binding activity with dissociation constants of 0.8 nM and 2 nM for aFGF and bFGF, respectively. Furthermore, binding of aFGF and bFGF to purified receptor resulted in self-phosphorylation, demonstrating that the isolated receptor had an unaltered intrinsic kinase activity.
http://www.hal.inserm.fr/inserm-00537599
Contributeur : Alicia Torriglia
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Soumis le : jeudi 18 novembre 2010 - 17:17:03
Dernière modification le : mardi 3 juillet 2018 - 09:34:10
Alicia Torriglia, Pierre Blanquet. Purification of an active receptor for acidic and basic fibroblast growth factor from bovine retina.. Biochimica et Biophysica Acta - Molecular Cell Research, Elsevier, 1992, 1137 (2), pp.215-24. 〈inserm-00537599〉
