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Purification and characterization of the 210‐amino acid recombinant basic fibroblast growth factor form (FGF‐2)
Author(s) -
Patry Véronique,
Bugler Béatrix,
Amalric François,
Promé Jean-Claude,
Prats Hervé
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00633-4
Subject(s) - edman degradation , amino acid , recombinant dna , microbiology and biotechnology , escherichia coli , biochemistry , fibroblast growth factor , biology , chemistry , peptide sequence , gene , receptor
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.