The heparin-binding growth factors aFGF and bFGF (acidic and basic fibroblast growth factor) from crude bovine brain extract were co-eluted with purified [125I]aFGF and/or [125I]bFGF as tracers from heparin-Sepharose and from several insoluble substituted polystyrenes used as stationary phases in low-pressure affinity chromatography. The ability of the resins to isolate FGFs was determined by measuring the eluted radioactivity. It was demonstrated that the various substituted polystyrene resins retain [125I]aFGF and [125I]bFGF with different specificities according to the chemical nature of the substituted groups bound to the polystyrene support. Bifunctional resins substituted with sulphonate and phenylalanine sulphamide groups adsorbed both [125I]aFGF and [125I]bFGF whereas bifunctional resins substituted with sulphonate and sulphamide serine adsorbed only [125I]bFGF. These stationary phases could be adapted to high-performance affinity chromatography and used to isolate growth factors of the FGF family.