Knoerzer W, Binder H P, Schneider K, Gruss P, McCarthy J E, Risau W
PROGEN Biotechnik GmbH, Heidelberg, F.R.G.
Gene. 1989 Jan 30;75(1):21-30. doi: 10.1016/0378-1119(89)90379-x.
Synthetic genes encoding bovine and human basic fibroblast growth factors (bFGFs) were assembled and cloned using established Escherichia coli expression plasmids. Transformed E. coli cells were able to synthesize either a fusion protein, comprising the first seven amino acids of beta-galactosidase, a linker fragment and bovine FGF, or genomic human bFGF. The two growth factors were purified from E. coli lysates by cation exchange and heparin-Sepharose affinity chromatography. The purified recombinant proteins were biologically active as monitored by their mitogenic activity for bovine aortic endothelial cells and their angiogenic capacity in the rabbit cornea.
