Xue Y, Wang H, Zhou T, Wang H, Wang F
Institute of Basic Medical Sciences, Beijing.
Chin Med Sci J. 1993 Dec;8(4):227-30.
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.
重组人酸性成纤维细胞生长因子（haFGF）通过肝素-琼脂糖亲和层析从大肠杆菌裂解物中纯化得到。纯化后的haFGF在刺激3T3细胞DNA合成方面表现出强大的促有丝分裂活性，并且肝素可显著增强该活性。通过对促有丝分裂活性和免疫特性的分析，发现haFGF与牛aFGF（baFGF）之间存在显著差异。主要差异在于haFGF对肝素的依赖性强于baFGF。
