Purification and characterization of the 210‐amino acid recombinant basic fibroblast growth factor form (FGF‐2)

FEBS Letters

Prats, Hervé²  Amalric, François¹  Bugler, Béatrix¹  Patry, Véronique²  Promé, Jean-Claude³ 

[1] Laboratoire de Biologie Moléculaire des Eucaryotes from Centre National de la Recherche Scientifique, 118 route de Narbonne, 31062 Toulouse, France;Unité 397 from Institut National de la Santé et de la Recherche Médicale, Institut Louis Bugnard, CHU Rangueil, Bât L3, 31054 Toulouse, France;Laboratoire de Spectrométrie de Masse et Signaux Biologiques from Centre National de la Recherche Scientifique, 205 route de Narbonne, 31077 Toulouse, France

关键词: Basic fibroblast growth factor;    High molecular weight form;    Recombinant protein;    E. coli;   

DOI  :  10.1016/0014-5793(94)00633-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown