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将狂犬病毒核蛋白结构基因重组到原核表达质粒ｐＭＡＬ－Ｃ_２Ｘ中，经ＩＰＴＧ诱导表达出的ＭＢＰ－ＮＰ融合蛋白分子量约 ９８ ｋＤ，用支链淀粉琼脂糖凝胶亲和层析纯化得到电泳均一的融合蛋白，融合蛋白用因子 Ｘａ裂解后，经 Ｑ－Ｓｅｐｈａｒｏｓｅ离子交换层析可将 ＭＢＰ与 ＮＰ分开，得到了电泳均一、分子量约 ５６ ｋＤ的 ＮＰ蛋白，经 Ｗｅｓｔｅｒｎ ｂｌｏｔ分析证实抗原性正确，为进一步利用ＮＰ蛋白制备抗体或单克隆抗体打下了基础。
The rabies virus nucleoprotein structural gene was recombined into the prokaryotic expression plasmid pMAL-C_2X, and the molecular weight of the MBP-NP fusion protein induced by IPTG was about 98 kD. The molecular weight of the MBP-NP fusion protein purified by amylose agarose gel electrophoresis was uniform After the fusion protein and the fusion protein were cleaved with factor Xa, MBP and NP were separated by Q-Sepharose ion exchange chromatography to obtain a homogeneous electrophoresis protein with a molecular weight of about 56 kD. Western blot analysis confirmed the antigenicity was correct The use of NP protein preparation of antibodies or monoclonal antibodies laid the foundation.