ACTA VETERINARIA ET ZOOTECHNICA SINICA ›› 2007, Vol. 38 ›› Issue (10): 1072-1076.doi:

• 预防兽医 • Previous Articles     Next Articles

Purification and Bioactivity Analysis of Porcine IL-4 Recombinant Protein

CHEN Guo-hua;JING Zhi-zhong;DOU Yong-xi;MENG Xue-lian;ZHANG Qiao-ying;SONG Shi-bin   

  1. Key Laboratory of Veterinary Parasitology of Gansu Province/State Key Laboratory of Veterinary Etiological Biology，Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046,China
  • Received:1900-01-01 Revised:1900-01-01 Online:2007-10-25 Published:2007-10-25

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Abstract: The recombinant expression vector pGEX-IL-4 was induced by IPTG in optimal conditions in E.coli.SDS-PAGE analysis showed that the expressed fusion protein with a molecular weight of 38 ku existed in the inclusion body. The fusion protein, which was of 25% in total bacterial proteins, was denatured, renatured, and purified with saturated ammonium sulfate precipitation and Sephadex-G100 with the purity of above 90%. MTT analysis indicated that purified protein has good bioactivity, which has laid a foundation for the production and development of recombinant protein of porcine IL-4.