[High-level expression of human acidic fibroblast growth factor in E. coli and its purification].
A reconstructed human acidic fibroblast growth factor (haFGF) cDNA was cloned into the expression vector pkk223-3, and the expression in Escherichia coli. JM109 was induced by IPTG induction; the expression level of the recombinant haFGF was about 80 mg/L. The expressed haFGF was purified to identity by heparin affinity chromatography and the recovery rate of haFGF was 65%. The specific activity of the purified haFGF was ED50 4.6 ng/ml. The characters of recombinant haFGF was identical to that of natural one.
Li
X
X
Chengdu Perfection Biotechnology Inc., Chengdu 610041.
Tu
C
C
Peng
H
H
Yuan
S
S
Wu
F
F
D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D016220:Fibroblast Growth Factor 1 / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification; D006801:Humans; D012333:RNA, Messenger / Q000096:biosynthesis / Q000235:genetics; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification
D004269:DNA, Bacterial; D012333:RNA, Messenger; D011994:Recombinant Proteins; D016220:Fibroblast Growth Factor 1