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目的建立高效、快速、简便的表达和纯化ＨＢｃＡｇ系统，为进一步研究ＨＢｃＡｇ在乙型肝炎发病机理中 的作用及 ＨＢＶ Ｃ基因变异产生 ＨＢｃＡｇ特征。方法应用 ｐＱＥ３０系统在原核细胞表达和纯化 ＨＢｃＡｇ。结果目的蛋 白表达量占细菌总蛋白的２６．２％；５００ｍｌ诱导表达的菌液可得平均５ｍｇ的ＨＢｃＡｇ；纯化的ＨＢｃＡｇ纯度可达到９１.０％； 免疫印迹分析，表达的ＨＢｃＡｇ具有多克隆抗－ＨＢｃ结合活性。结论建立了一套高效、快速表达和纯化ＨＢｃ Ａｇ系统。
Objective To establish an efficient, rapid and easy expression and purification of HBcAg system for further study of the role of HBcAg in the pathogenesis of hepatitis B and HBV C gene mutation characteristics of HBcAg. Methods The pQE30 system was used to express and purify HBcAg in prokaryotic cells. RESULTS: The expressed protein accounted for 26.2% of the total bacterial protein. The average volume of HBcAg purified by the method of 500ml induced bacterial culture was 5mg. The purity of purified HBcAg was 91.0%. The immunoblot analysis showed that the expressed HBcAg had polyclonal antibody -HBc binding activity. Conclusion A set of efficient, rapid expression and purification HBc Ag system was established.