FEBS Letters | |
Human brain fibroblast growth factor | |
Esch, Frederick1  Böhlen, Peter1  Jones, Kenneth L.1  Baird, Andrew1  Gospodarowicz, Denis1  | |
[1] Laboratories for Neuroendocrinology, The Salk Institute for Biological Studies, La Jolla, CA 92138 U.S.A. | |
关键词: Heparin-Sepharose affinity chromatography; HPLC; Microsequencing; Endothelial cell proliferation; Radioimmunoassay; | |
DOI : 10.1016/0014-5793(85)80765-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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-PhePro-. This sequence is identical to that of the amino-terminal region of bovine FGF. Additional evidence, including amino acid composition, Chromatographie retention behavior, and immunoreactivity suggest that the human and bovine mitogens are very similarin structure.
【 授权许可】
Unknown
【 预 览 】
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RO201912020286799ZK.pdf | 476KB | download |