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《Chinese Journal of Animal and Veterinary Sciences》 2004-01
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Prokaryotic Expression of ORF5 Gene of PRRS Virus BJ-4 and Purification of Recombinant Protein

GU Hong,YANG Han-chun,GUO Xin,CHEN Yan-hongne,Ministry of Agriculture,China Agricultural University,Beijing 100094,China)  
In order to successfully express the structural protein GP5 of porcine reproductive and respiratory syndrome virus(PRRSV),the gene segment dORF5 deleting N-terminal very hydrophobic sequence were successfully amplified from recombinant plasmid pGEM-ORF5 by PCR and were cloned into prokaryotic expression vector pGEX-4T-2.The recombinant fusion proteins GST-dORF5 were highly expressed in E coli.cell BL21 in the forms of inclusion bodies and could amount to 20.8% of the total mass of bacterial proteins.Western-Blot showed the recombinant protein could react with the porcine polyclonal antibodies against PRRSV.Recombinant proteins were purified and renatured.The purity of recombinant proteins affinity-purified using Glutathione Sepharose 4B were above 90%.The studies provided fundamental data and materials for the further study on the structure and function of structural proteins of PRRSV.
【Fund】: 霍英东青年教师基金(71032)
【CateGory Index】: S858.28
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