Human brain fibroblast growth factor. Isolation and partial chemical characterization.
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.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001013:Aorta, Thoracic; D001681:Biological Assay; D001923:Brain Chemistry; D002417:Cattle; D002455:Cell Division; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D004727:Endothelium / Q000166:cytology; D005346:Fibroblast Growth Factors / Q000302:isolation & purification* / Q000494:pharmacology; D006801:Humans; D011863:Radioimmunoassay
D000596:Amino Acids; D005346:Fibroblast Growth Factors