title: [High-level expression of human acidic fibroblast growth factor in E. coli and its purification].
abstract: 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.
authors.affiliation: Chengdu Perfection Biotechnology Inc., Chengdu 610041.
authors.forename: X
authors.initials: X
authors.lastname: Li
authors.forename: C
authors.initials: C
authors.lastname: Tu
authors.forename: H
authors.initials: H
authors.lastname: Peng
authors.forename: S
authors.initials: S
authors.lastname: Yuan
authors.forename: F
authors.initials: F
authors.lastname: Wu
mesh_terms: 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
chemical_list: D004269:DNA, Bacterial; D012333:RNA, Messenger; D011994:Recombinant Proteins; D016220:Fibroblast Growth Factor 1