Böhlen P, Esch F, Baird A, Jones K L, Gospodarowicz D
FEBS Lett. 1985 Jun 3;185(1):177-81. doi: 10.1016/0014-5793(85)80765-1.
Fibroblast growth factor (FGF) has been purified to homogeneity from human brain by a procedure involving salt precipitation, cation-exchange chromatography, Heparin-Sepharose affinity chromatography and reverse-phase HPLC. Isolation was monitored by radioimmunoassay and/or by testing column fractions for their capacity to stimulate the proliferation of vascular endothelial cells in vitro. The amino-terminal sequence of human brain FGF was determined as Pro-Ala-Leu-Pro-Glu-Asp-Gly-Gly-Ser-Gly-Ala-Phe-Pro-. This sequence is identical to that of the amino-terminal region of bovine FGF. Additional evidence, including amino acid composition, chromatographic retention behavior, and immunoreactivity suggest that the human and bovine mitogens are very similar in structure.
通过盐沉淀、阳离子交换色谱、肝素-琼脂糖亲和色谱和反相高效液相色谱等步骤，已从人脑中纯化出具有同质性的成纤维细胞生长因子（FGF）。通过放射免疫测定和/或检测柱级分在体外刺激血管内皮细胞增殖的能力来监测分离过程。人脑FGF的氨基末端序列确定为Pro-Ala-Leu-Pro-Glu-Asp-Gly-Gly-Ser-Gly-Ala-Phe-Pro-。该序列与牛FGF氨基末端区域的序列相同。包括氨基酸组成、色谱保留行为和免疫反应性在内的其他证据表明，人和牛的促细胞分裂剂在结构上非常相似。
