Amino acid sequence of human acidic fibroblast growth factor |
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| Authors: | P Gautschi-Sova T Müller P B?hlen |
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| Affiliation: | 1. Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, Ontario M5S 3E5, Canada;2. Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, 160 College Street, Toronto, Ontario M5S 3E1, Canada;3. Department of Pharmaceutical Chemistry, University of California − San Francisco, 1700 Fourth Street, San Francisco, CA 94158-2550, United States;4. Institute of Biomaterials and Biomedical Engineering, 164 College Street, Toronto, Ontario M5S 3G9, Canada;5. Department of Chemistry, University of Toronto, 80 St. George Street, Toronto, Ontario M5S 3H6, Canada;1. School of Chemistry, Chemical Engineering, and Life Science, Wuhan University of Technology, Wuhan 430070, PR China;2. Shaoxing Institute for Advanced Research, Wuhan University of Technology, Shaoxing 312300, PR China;3. School of Information Engineering, Wuhan University of Technology, Wuhan 430070, PR China;4. Institut WUT-AMU, Wuhan University of Technology, Wuhan 430070, PR China;5. State Key Laboratory of Silicate Materials for Architectures, Wuhan University of Technology, Wuhan 430070, PR China;6. Sanya Science and Education Innovation Park, Wuhan University of Technology, Sanya 572024, PR China;7. School of Resources and Environmental Engineering, Wuhan University of Technology, Wuhan 430070, PR China;8. School of Materials Science and Engineering, Wuhan University of Technology, Wuhan 430070, PR China |
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| Abstract: | The complete amino acid sequence of human brain acidic fibroblast growth factor (aFGF) has been established. Human aFGF consists of 140 amino acids and is highly homologous to bovine aFGF (11 amino acid replacements). Results from experiments involving alkylation of cysteine residues are compatible with the possibilities that in aFGF all three cysteines exist as free sulfhydryls, or alternatively, that a disulfide bridge is present but cannot be identified due to disulfide scrambling caused by the SH group of the remaining cysteine. A potential glycosylation site Asn114-Gly115-Ser116 is present in aFGF but the mitogen does not bind to lectins suggesting that it may not be glycosylated. |
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