| 原核表达的猪瘟病毒E2蛋白抗原多肽的复性和纯化 |
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| 引用本文： | 刘伯华,余兴龙,张茂林,肖昌,徐兴然,吴健敏,李作生,涂长春.原核表达的猪瘟病毒E2蛋白抗原多肽的复性和纯化[J].中国兽医学报,2003,23(2):145-148. |
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| 作者姓名： | 刘伯华 余兴龙 张茂林 肖昌 徐兴然 吴健敏 李作生 涂长春 |
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| 作者单位： | 解放军军需大学军事兽医研究所,吉林,长春,130062 |
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| 基金项目： | 国家“973”项目 (G19990 1190 3 ) |
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| 摘 要： | 对原核中以包涵体形式高效表达的猪瘟病毒（CSFV）E2蛋白抗原表位区段（mE2)进行了变性、复性与纯化研究。包涵体经超声破菌分离，然后进行变性溶解和复性，复性产物经硫酸铵沉淀浓缩后，利用免疫亲和层析进行纯化。纯化产物SDS－PAGE分析结果表明，其纯度达97％。酶联免疫试验测定的结果显示，与复性前变性蛋白相比，纯化蛋白与CSFV特异的单抗和多克隆阳性血清的反应活性提高了2－16倍。
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| 关 键 词： | 原核表达 猪瘟病毒 E2蛋白抗原多肽 包涵体 复性 纯化 保护性抗原蛋白 |
| 文章编号： | 1005-4545(2003)02-0145-04 |
| 修稿时间： | 2001年10月8日 |
Renaturation and Purification of E. coli-expressed CSFV Antigenic Polypeptide |
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| Abstract: | The highly antigenic polypeptide of CSFV E2 protein (refered to mE2) expressed as insoluble form of inclusion body in E.coli was prepared by sonication of the bacterial cells and then subjucted to denaturation followed by renaturation.The renaturated product was further concentrated by ammonium sulphate before purification using immunological affinity chromatography, which eventually resulted in 97% of purity of mE2 protein. The reactivity of purified mE2 with a panel of CSFV-specific monoclonal and polyclonal antibodies was increased 2-16 times in ELISA after renaturation of the denatured protein. |
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| Keywords: | classical swine fever virus E2 protein antigenic polypeptide inclusion bodies renaturation purification |
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