Biopolymers and cell. 2003; 19 (2): 179 - 184

Biosynthesis of human basic fibroblast growth factor in soluble form in Escherichia coli and its purification

I. Yu Slavchenko, E. V. Boreyko, T. C. Gavrysh, I. P. Kostyuchenko, V. A. Kordyum

Basic fibroblast growth factor (bFGF, also known as FGF-2) is an important modulator of cell differentiation, proliferation, migration, migration, angiogenesis and other activities in a variety of cell types. The recombinant human bFGF is considered as a potential medicine for the treatment of vascular and some other diseases. In this work the production of human bFGF of 146 a. a. length, in E. coli cells, using the phage lambda, and its purification have been elaborated. The method of recombinant protein production includes the phage lambda infection of the BL21 (DE3) cells, containing a plasmid with a target gene under the T7 phage promoter. The process results in lysis of the producer strain cells and releasing newly synthesized bFGF into the cell medium, where it accumulates in a soluble form (approximately 60 mg/l). The target protein has been purified to homogeneity not less than 98 % by a one-step procedure using heparin-Sefarose affinity chromatography. According to the biological tests bFGF obtained promotes angiogenesis in chick embryo chorioallantoic membrane.