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pubmed-article:2470650pubmed:abstractTextSynthetic 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.lld:pubmed
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pubmed-article:2470650pubmed:articleTitleExpression of synthetic genes encoding bovine and human basic fibroblast growth factors (bFGFs) in Escherichia coli.lld:pubmed
pubmed-article:2470650pubmed:affiliationPROGEN Biotechnik GmbH, Heidelberg, F.R.G.lld:pubmed
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