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构建了丙型肝炎病毒核心蛋白的全长（ａａ１～１９１）及Ｎ端（ａａ１～６９）和Ｎ端（ａａ１～４０）与谷胱甘肽巯基转移酶（ＧＳＴ）的融合表达克隆，比较了在不同大肠杆菌中的表达。表达蛋白为水溶性。经ＥＬＩＳＡ和蛋白质印迹分析，ＧＳＴＣ１９１的表达和稳定性都较差，ＧＳＴＣ６９和ＧＳＴＣ４０具有良好的稳定性，用ＧＳＴ亲和柱一步纯化，纯度可达９０％，免疫小鼠可产生高滴度的抗体。应用表达的ＧＳＴＣ６９和ＧＳＴＣ４０抗原，检测人血清中的ＨＣＶ核心蛋白抗体，初步结果显示具有良好的特异性。
The full-length (aa1 ~ 191) and fusion clones of N-terminal (aa1 ~ 69) and glutathione S-transferase (GST) of hepatitis C virus core protein were constructed and compared Expression in different E. coli. The expressed protein is water-soluble. The expression and stability of GSTC191 were poorly expressed by ELISA and Western blot analysis. GSTC69 and GSTC40 showed good stability. Purified by GST affinity column, the purity of GSTC191 was 90%. Immunized mice produced high titer antibody . The initial detection of HCV core protein antibodies in human serum using the expressed GSTC69 and GSTC40 antigens showed good specificity.