Patry V, Bugler B, Amalric F, Promé J C, Prats H
Unité 397 from Institut National de la Santé et de la Recherche Médicale, Institut Louis Bugnard, CHU Rangueil, Toulouse, France.
FEBS Lett. 1994 Jul 25;349(1):23-8. doi: 10.1016/0014-5793(94)00633-4.
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.
