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- W2354845707 abstract "Objective To express fusion human insulin-like growth factor-1(hIGF-1)in prokaryotic cells,and purify and identify the expressed product. Methods The sequence of natural hIGF-1 gene was subjected to samesense mutation according to the E. coli preferred codons,synthesized amplified by PCR and cloned into vector pET48b(+). The construct recombinant plasmid pET48b-Trx A-hIGF-1 was transformed to E. coli BL21(DE3) for expression under induction of IPTG. The expressed fusion protein Trx A-hIGF-1 was purified by nickel ion affinity chromatography,digested with enterokinase and identified by SDS-PAGE. Results Recombinant plasmid pET48b-Trx A-hIGF-1 was constructed correctly as proved by colony PCR and sequencing. The expressed fusion protein, with a relative molecular mass of about 26 000, contained about 40% of total somatic protein and mainly existed in a soluble form,of which the proportion of soluble protein to total target protein was not less than 90%. The fusion protein reached a purity of not less than 90% and a concentration of 0. 5 mg / ml,which was digested with enterokinase into hIGF-1 with a relative molecular mass of about 8 000 and Trx A with a relative molecular mass of about 18 000. The hIGF-1 showed specific binding to rabbit anti-hIGF-1 polyclonal antibody. Conclusion The hIGF-1 fusion protein was successfully expressed,which laid a foundation of study on biological activity and large-scale production of hIGF-1." @default.
- W2354845707 created "2016-06-24" @default.
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- W2354845707 date "2013-01-01" @default.
- W2354845707 modified "2023-09-22" @default.
- W2354845707 title "Fusion expression and purification of human insulin-like growth factor-1" @default.
- W2354845707 hasPublicationYear "2013" @default.
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