| 结核杆菌Ag85B的表达纯化 |
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| 引用本文： | 智刚,王宝林,季朝能,朱琪泉,王洪海. 结核杆菌Ag85B的表达纯化[J]. 复旦学报(自然科学版), 2002, 41(1): 113-116 |
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| 作者姓名： | 智刚 王宝林 季朝能 朱琪泉 王洪海 |
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| 作者单位： | 复旦大学生命科学学院,上海,200433 |
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| 摘 要： | 为构建抗结核病新型疫苗，以结核杆菌标准毒力株H37Rv DNA为模板，用PCR法克隆抗原85B的编码基因，将该基因重组到表达型质粒pQE30中，表达的His6 Tag-Ag85B融合蛋白分子质量约32ku，用亲和层析一步法纯化的重组蛋白纯度好，得率高，为进一步的免疫研究创造了条件。
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| 关 键 词： | 结核杆菌 抗原85B 基因表达 |
| 文章编号： | 0427-7104(2002)01-0113-04 |
The Expression and Purification of Ag85B of Mycobacterium Tuberculosis |
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| ZHI Gang,WANG Bao lin,JI Chao neng,ZHU Qi quan,WANG Hong hai. The Expression and Purification of Ag85B of Mycobacterium Tuberculosis[J]. Journal of Fudan University(Natural Science), 2002, 41(1): 113-116 |
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| Authors: | ZHI Gang WANG Bao lin JI Chao neng ZHU Qi quan WANG Hong hai |
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| Abstract: | Using virulent strain of Mycobacterium tuberculosis,H37Rv, as template, the coding sequence of mature Ag85B was cloned in pQE30 by PCR. The recombinant protein from the extracts of stable transfected TG1 was purified by one step affinity chromatography. The molecular mass of the product, with RGS His6 tag, is 32 ku. The purity and quantity of the purified recombinant protein is satisfactory, which will assist further research work on Ag85B. |
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| Keywords: | mycobacterium tuberculosis Ag85B gene expression |
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