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Virologica Sinica, 19 (2) : 101-104, 2004
Research Article
Purification and Observation of the Recombinant Hepatitis B Virus Core Antigen (rHBcAg) Particles Produced in the Yeast
1.School of Life Science and Biotechnology, Shanghai Jiaotong University, Shanghai 200030,China
2. School of Life Science, Shanghai University, Shanghai 200436,China
3. Biological Technology Center of Shanghai Agriculture Science Institute, Shanghai 201106,China
 Correspondence:
(224.05KB)  
Abstract
Hepatitis B virus core antigen protein gene (C gene) was expressed in Saccharomyces cerevisiae and the products (rHBcAg particles) were purified from crude lysate of the yeast by three steps: Sephrose CL-4B chromatography, sucrose step-gradient ultracentrifugation, and CsCl-isopycnic ultracentrifugation. rHBcAg was synthesized in yeast cells as a particle consisting of polypeptides which have a molecular weight of 21.5 kDa (p21.5). ELISA and CsCl- isopycnic ultracentrifugation purification products (rHBcAg particles) in each fraction indicated that the particle densities of the fraction with higher rHBcAg antigenicity mainly distributed at the densities of 1.27g•mL-1 and 1.40 g•mL-1, respectively. Observation of the purified products (rHBcAg particles) by TEM indicated that rHBcAg peptides could self-assemble into two kinds of different sizes of rHBcAg particles (core particles); the large particle was about 30.1±2.4 nm in diameter and the small particle about 21.5±3.3 nm. This indicated that the rHBcAg particles displayed dimorphism, but the biological significance of this dimorphism is not clear and needs to be studied further.
  Published online: 20 Apr 2004
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