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Volume 14 Issue 3
June 1999
    Citation: Lei-Yin-Beng, LIN Yu-Lin, TAO Hua-Jun, JIAN Ai-Zhen, LI Hui, ZHANG Wei-Yang. Separation，Purification and Identification of Structural Proteins of Hepatitis A Virus .VIROLOGICA SINICA, 1999, 14(3) : 210-216.
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    Separation，Purification and Identification of Structural Proteins of Hepatitis A Virus

    • 1.

      Department Virology，Union Hospital Tongfi Medical University，Wuhan 430022

    • 2.

      Virtu Rts~rch Instituy, Hubel Medical University, Wuhann 430071

    • Available online: 05 September 1999
    • A cell line persistently infected by Hepatitis A virus (HAV) was ultilized to produce high yield viral particles of HAV. HAV particles were recovered in a single ultracentrifugation step through discontinuous sucrose/glycerol density gradients. Three kinds of major structural protein of HAV were separated and purified by high performance liquid chormatography. SDS PAGE demonstrated the molecular weight of three structural proteins of HAV being 33, 29 and 27?kD. The special immune reactions were shown in Western blot test, suggesting the proteins with 33, 29 and 27?kD are VP\-1, VP\-2 and VP\-3 of the virus, respectively. The total contents of the proteins, VP\-1, VP\-2 and VP\-3 were respectively 687, 220.8, 68 and 213.6?g from 11?200?cm\+2 cells infected with HAV. The highly purified particles and sturctural proteins of HAV may be used in research for the development of vaccine, clinical diagnosis and pathogenesis of HAV.
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      Separation，Purification and Identification of Structural Proteins of Hepatitis A Virus

      • 1. Department Virology，Union Hospital Tongfi Medical University，Wuhan 430022
      • 2. Virtu Rts~rch Instituy, Hubel Medical University, Wuhann 430071

      Abstract: A cell line persistently infected by Hepatitis A virus (HAV) was ultilized to produce high yield viral particles of HAV. HAV particles were recovered in a single ultracentrifugation step through discontinuous sucrose/glycerol density gradients. Three kinds of major structural protein of HAV were separated and purified by high performance liquid chormatography. SDS PAGE demonstrated the molecular weight of three structural proteins of HAV being 33, 29 and 27?kD. The special immune reactions were shown in Western blot test, suggesting the proteins with 33, 29 and 27?kD are VP\-1, VP\-2 and VP\-3 of the virus, respectively. The total contents of the proteins, VP\-1, VP\-2 and VP\-3 were respectively 687, 220.8, 68 and 213.6?g from 11?200?cm\+2 cells infected with HAV. The highly purified particles and sturctural proteins of HAV may be used in research for the development of vaccine, clinical diagnosis and pathogenesis of HAV.

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