| EB病毒核抗原1羧基端原核表达产物的纯化方法 |
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| 引用本文： | 王卫东,齐建国,谷淑燕.EB病毒核抗原1羧基端原核表达产物的纯化方法[J].湖北师范学院学报(自然科学版),2005,25(1):10-12,19. |
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| 作者姓名： | 王卫东 齐建国 谷淑燕 |
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| 作者单位： | 1. 湖北师范学院,生物系,湖北,黄石,435002
2. 中国疾病预防控制中心病毒病预防控制所,北京,100052 |
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| 摘 要： | EB病毒核抗原1羧基端的原核表达产物以包涵体和可溶性两种形式存在,用镍离子亲和柱分别对其进行了纯化.结果显示,可溶性部分以及经2M尿素溶解后的包涵体的最适咪唑洗脱浓度均为150mM.纯化后重组蛋白的纯度在90%以上.
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| 关 键 词： | EB病毒核抗原1 原核表达 纯化 |
| 文章编号： | 1009-2714(2005)01-0010-03 |
Purification of carboxyl-terminal domain of epstein-barr virus nuclear antigen 1 expressed in E. Coli |
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| WANG Wei-dong,QI Jian-guo,GU Shu-yan.Purification of carboxyl-terminal domain of epstein-barr virus nuclear antigen 1 expressed in E. Coli[J].Journal of Hubei Normal University(Natural Science),2005,25(1):10-12,19. |
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| Authors: | WANG Wei-dong QI Jian-guo GU Shu-yan |
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| Institution: | WANG Wei-dong1,QI Jian-guo2,GU Shu-yan2 |
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| Abstract: | A fusion protein, which contains carboxyl-terminal domain of Epstein-Barr virus nuclear antigen 1, was expressed in E. coli BL21 (DE3). After induction with IPTG, samples analysis results revealed that the fusion protein was approximately 25 kD in size (25-kD EBNA1), and it occurred both in the form of inclusion bodies and soluble protein. Both the soluble protein and the inclusion bodies solved in 2M urea could be purified with Ni 2+ affinity chromatography. The optimum eluting concentrations of imidazole are both 150mM. The estimated purity of purified 25-kD EBNA1 is upon 90%. |
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| Keywords: | EBNA1 prokaryotic expression purification |
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