Citation: CAI Mei-hong, CAO Rui-bing, ZHOU Bin, TAN Guo-lei, YANG Song, CHEN Pu-yan. Expression of the Mature Protein Gene of Chicken γ-Interferon and the Detection for the Antiviral Activity of the Purified Expression Product .VIROLOGICA SINICA, 2004, 19(1) : 32-35.

Expression of the Mature Protein Gene of Chicken γ-Interferon and the Detection for the Antiviral Activity of the Purified Expression Product

  • Corresponding author: CHEN Pu-yan, 
  • Available online: 20 February 2004
  • Using the total mRNA in the lymphocyte in chicken blood as the template, the mature protein gene of interferon γ-interferon was cloned and amplified through the reverse transcription polymerase chain reaction. The gene was then ligated to pRLC to establish the gene’s non-fusion expressing vector. The best inducing time for the expression of this recombinant protein was tested through inducing the expression of positive selected plasmid with different time span. This expressed product was then denatured and renatured and was added to the culture medium with CEF, which were attacked by the 100 TCID50 VSV. The result showed that the activity of the recombinant protein was up to 1.0×106 U/mg.

  • 加载中
  • 加载中

Article Metrics

Article views(3634) PDF downloads(954) Cited by()

Related
Proportional views

    Expression of the Mature Protein Gene of Chicken γ-Interferon and the Detection for the Antiviral Activity of the Purified Expression Product

      Corresponding author: CHEN Pu-yan,
    • 1. 1. Key Laboratory of Animal Diseases Diagnosis & Immunology of China’s Department of Agriculture, Nanjing Agricultural University, Nanjing 210095, China
    • 2. Department of Veterinary medicine,Shenyang Agricultural University, Shenyang 110161, China

    Abstract: Using the total mRNA in the lymphocyte in chicken blood as the template, the mature protein gene of interferon γ-interferon was cloned and amplified through the reverse transcription polymerase chain reaction. The gene was then ligated to pRLC to establish the gene’s non-fusion expressing vector. The best inducing time for the expression of this recombinant protein was tested through inducing the expression of positive selected plasmid with different time span. This expressed product was then denatured and renatured and was added to the culture medium with CEF, which were attacked by the 100 TCID50 VSV. The result showed that the activity of the recombinant protein was up to 1.0×106 U/mg.

    Relative (20)

    目录

    /

    DownLoad:  Full-Size Img  PowerPoint
    Return
    Return