Purification and characterization of the 210-amino acid recombinant basic fibroblast growth factor form (FGF-2).
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.
Patry
V
V
Unité 397 from Institut National de la Santé et de la Recherche Médicale, Institut Louis Bugnard, CHU Rangueil, Toulouse, France.
Bugler
B
B
Amalric
F
F
Promé
J C
JC
Prats
H
H
D000595:Amino Acid Sequence; D001483:Base Sequence; D002455:Cell Division; D002478:Cells, Cultured; D004926:Escherichia coli / Q000235:genetics; D016222:Fibroblast Growth Factor 2 / Q000235:genetics* / Q000302:isolation & purification* / Q000494:pharmacology; D014644:Genetic Variation; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000302:isolation & purification; D017421:Sequence Analysis
D011994:Recombinant Proteins; D016222:Fibroblast Growth Factor 2