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- W2347969813 abstract "Objective To express Trichinella pseudospiralis serine proteinase inhibitor(Tp-serpin)gene in prokaryotic cells,purify the expressed product and identify its antigenicity. Methods Tp-serpin gene was amplified by RT-PCR from total RNA of muscle larvae of Tp and inserted into prokaryotic expression vector pET-28a(+). The constructed recombinant plasmid pET-28a-Tp-serpin was transformed to E. coli Rosetta gami(DE3)and induced by IPTG. The expressed product was identified by SDS-PAGE,purified by Ni-NTA Agarose affinity chromatography,then analyzed for purity by SDS-PAGE,and for reactogenicity by Western blot. Results PCR,restriction analysis and sequencing proved that recombinant plasmid pET-28a-Tp-serpin was constructed correctly,in which the target gene fragment showed a homology of 99% to the Tp-serpin gene in GenBank. The expressed recombinant protein,with a relative molecular mass of about 43 000,contained about 40% of total somatic protein,mainly existed in a soluble form,reached a purity of more than 95% after purification,was recognized specifically by porcine serum infected with Tp for 60 d,and showed good reactogenicity. Conclusion Recombinant plasmid pET-28a-Tp-serpin was constructed successfully,and recom-binant protein Tp-serpin was expressed in E. coli Rosetta gami(DE3),which provided a scientific basis for the development of antigen for serologic diagnosis of trichinosis and investigation of role of serpin in regulating the host immune response during the invasion period of Tp." @default.
- W2347969813 created "2016-06-24" @default.
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- W2347969813 date "2014-01-01" @default.
- W2347969813 modified "2023-09-26" @default.
- W2347969813 title "Prokaryotic expression and purification of Trichinella pseudospiralis serine proteinase inhibitor" @default.
- W2347969813 hasPublicationYear "2014" @default.
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