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  • Title: Purification and characterization of the 210-amino acid recombinant basic fibroblast growth factor form (FGF-2).
    Author: Patry V, Bugler B, Amalric F, Promé JC, Prats H.
    Journal: FEBS Lett; 1994 Jul 25; 349(1):23-8. PubMed ID: 8045296.
    Abstract:
    Four forms of basic fibroblast-growth factor (bFGF or FGF-2) using one AUG (155 amino acids) and three upstream CUG (210, 201 and 196 amino acids) start codons, were synthesized through an alternative use of initiation codons. The 210-amino acid form of FGF-2 (210FGF-2) was expressed in a plasmid vector under the control of a bacteriophage T7 RNA polymerase promoter system in Escherichia coli. Characterization of the purified protein was performed by electrospray mass spectrometry and Edman degradation. The recombinant 210FGF-2 produced in E. coli had a mitogenic activity similar to the 146-amino acid form extracted from tissues.
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