Purification of an active receptor for acidic and basic fibroblast growth factor from bovine retina

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.