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HSV-1包膜糖蛋白G重组蛋白的纯化与抗原性分析 被引量:1

THE PURIFICATION OF THE PROKARYOTIC EXPRESSION CLONE OF HSV-1 GLYCOPROTEIN G AND ANTIGENIC ANALYSIS
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摘要 ①目的 纯化原核表达的HSV 1包膜糖蛋白G重组蛋白并对其抗原性进行分析。②方法 应用亲和层析法纯化重组蛋白 ,Western印迹和ELISA法检测分析其抗原性。③结果 Western Blot检测 15份HSV 1IgM阳性血清 ,其中 12份血清可与重组蛋白发生反应 ;ELISA法检测 5 35份血清 ,与商品化同类试剂盒相比符合率为 89.7% .④结论 该重组蛋白检测HSV 1活动性感染有较高的应用价值。 Objective\ To purify the recombinant HSV 1 glycoprotein G and analyse its antigenicity. \ Methods\ The recombinant protein was purified with affinity chromatography and the antigenicity was analyzed by Western Blot and ELISA. Results\ The recombinant protein could react with 12 samples of 15 HSV 1 IgM positive serum. 535 serum samples were detected by ELISA. Comparing with commercial ELISA kit,the agreement rate was 89.7%.\ Conclusion\ The recombinant protein has high value for detecting HSV 1 active infection.
出处 《青岛大学医学院学报》 CAS 2002年第2期130-132,共3页 Acta Academiae Medicinae Qingdao Universitatis
基金 山东省卫生厅科研基金资助项目 (9810 80 10 2 )
关键词 重组蛋白质类 纯化 酶联免疫吸附测定 recombinant proteins purification enzyme linked immunosorbent assay
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