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Production and characterization of human basic fibroblast growth factor from Escherichia coli.

作者信息

Squires C H, Childs J, Eisenberg S P, Polverini P J, Sommer A

机构信息

Synergen, Inc., Boulder, Colorado 80301.

出版信息

J Biol Chem. 1988 Nov 5;263(31):16297-302.

PMID:3053689
Abstract

The cDNA sequence coding for human basic fibroblast growth factor (bFGF) has been cloned downstream of a transcription promoter recognized by the bacteriophage T7 RNA polymerase. Initiation of translation at the fgf gene has been coupled to upstream translation of a fragment of the T7 phi 10 gene. Expression of the fgf gene in this system can lead to an accumulation of approximately 40 mg/liter/A600 unit of bFGF. This material can be purified close to homogeneity from a soluble protein extract on a heparin-Sepharose column. bFGF so obtained has been shown to have bioactivity indistinguishable from human placental fibroblast growth factor in mitogenicity, synthesis of plasminogen activator, and angiogenesis assays.

摘要

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