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Hepatitis B virus preS1에 대한 생쥐 단일클론항체의 제조와 특성연구
김윤규,김희선,류춘제,진병래,홍효정 大韓免疫學會 1996 大韓免疫學會誌 Vol.18 No.3
To generate a murine monoclonal antibody (mAb) to the preSi antigen of hepatitis B virus (HBV), preSi fusion proteins maltose binding protein (MBP)-preSl and glutathione S-transferase (GST)-preSl/preS2 were expressed in Escherichia coli in a soluble form and purified from the cell lysate. Each fusion protein was immunized into BALB/c mice and the resulting antisera were titrated for the antibody to the preSi antigen. The result showed that the immunogenicity of the MBP-preSi was more effective than that of the GST preSi/preS2. Six hybridoma clones secreting good amount of the mAb were isolated and the isotype of each mAb was determined, which showed that two were IgGl and four were IgM. Among them, 1B3 antibody (IgGl), derived from the mice immunized with the MBP-preSi, was purified from the culture supernatant of the hybridoma and characterized. The purified 1B3 bound to the preSi in a dose-dependent manner and immunoprecipitated HBV particles as almost efficiently as anti-S and anti-preS2 mAbs which were previously shown to have the in vitro neutralizing activity for HBV. These results indicate that the MBP-preSl fusion protein can be an useful immunogen for the generation of the anti-preSi murine mAb and the 1B3 mAb may be useful to the fundamental and applied researches related with HBV.