| 蜘蛛杀虫肽与Bt-toxin C肽融合蛋白(BGT)基因的原核表达与蛋白质纯化 |
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| 引用本文： | 孙冬,詹亚光,曾凡锁. 蜘蛛杀虫肽与Bt-toxin C肽融合蛋白(BGT)基因的原核表达与蛋白质纯化[J]. 植物生理学通讯, 2007, 43(5): 869-872 |
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| 作者姓名： | 孙冬 詹亚光 曾凡锁 |
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| 作者单位： | 东北林业大学生命科学学院 哈尔滨150040 |
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| 摘 要： | 从质粒pCAMBIA2301-BGT中获得蜘蛛杀虫肽与Bt-toxin C肽融合蛋白(BGT)基因编码区全长,并构建了原核表达载体pET28a-BGT。将此质粒转入大肠杆菌BL21(DE3)中,获得有效表达,新蛋白的分子量约为51 kDa,主要以包涵体形式存在。在变性条件下以不同的咪唑和pH值洗脱方式进行比较,确定以咪唑为金属鳌合亲和柱层析的洗脱条件,获得了纯BGT蛋白。
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| 关 键 词： | 蜘蛛杀虫肽 原核表达 蛋白纯化 |
| 修稿时间： | 2007-05-30 |
Prokaryotic Expression and Protein Purification of Spider Insecticidal Peptide and Bt-toxin C Peptide Gene |
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| SUN Dong,ZHAN Ya-Guang,ZENG Fan-Suo. Prokaryotic Expression and Protein Purification of Spider Insecticidal Peptide and Bt-toxin C Peptide Gene[J]. Plant Physiology Communications, 2007, 43(5): 869-872 |
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| Authors: | SUN Dong ZHAN Ya-Guang ZENG Fan-Suo |
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| Abstract: | The complete sequence of BGT gene was amplified from the plasmid pCAMBIA2301-BGT,and the prokaryotic expression vector of pET28a-BGT was constructed successfully.The recombinant vector pET28a- BGT was transformed into Esherichia coli BL21(DE3)and expressed in efficiency.The expressed protein was in the form of inclusion bodies with the molecular weight 51 kDa.Different pH and imidazole elution methods were investigated for the purification of BGT fusion protein by immobilized metal ion affinity chromatography under denaturing conditions,showing that imidazole was better,and the electrophoresis purity BGT protein was acquired. |
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| Keywords: | Bt |
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