Characterization of recombinant human acidic fibroblast growth factor: comparative studies with bovine acidic fibroblast growth factor.

Recombinant human acidic fibroblast growth factor (haFGF) was purified from E. coli lysate by heparin-sepharose affinity chromatography. The purified haFGF exhibited potent mitogenic activity in stimulating DNA synthesis in 3T3 cells and this activity could be significantly increased by heparin. By analysis of mitogenic activity and immunological properties, a marked difference was found between haFGF and bovine aFGF (baFGF). The main difference was that the heparin-dependence of haFGF was stronger than that of baFGF.