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Human brain fibroblast growth factor. Isolation and partial chemical characterization.

Authors
  • Böhlen, P
  • Esch, F
  • Baird, A
  • Jones, K L
  • Gospodarowicz, D
Type
Published Article
Journal
FEBS Letters
Publisher
Wiley (John Wiley & Sons)
Publication Date
Jun 03, 1985
Volume
185
Issue
1
Pages
177–181
Identifiers
PMID: 3996594
Source
Medline
License
Unknown

Abstract

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.

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