| H5N1亚型禽流感基质蛋白M1基因的原核表达和纯化 |
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| 引用本文： | 储结园,王海军,王春雨,陈迪,王全凯. H5N1亚型禽流感基质蛋白M1基因的原核表达和纯化[J]. 经济动物学报, 2010, 14(1): 26-29 |
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| 作者姓名： | 储结园 王海军 王春雨 陈迪 王全凯 |
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| 作者单位： | 1. 吉林农业大学中药材学院,长春,130118
2. 吉林农业大学国际合作与交流处,长春,130118 |
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| 摘 要： | 为获得纯度大于90%的M1蛋白,构建重组质粒PET-22b-M1,将正确的重组质粒转化到大肠杆菌BL21(DE3)中,IPTG诱导表达,经SDS-PAGE检测分析表达形式和表达量,并经Ni2+柱亲和层析与柱层析纯化表达蛋白。结果表明:试验成功构建了pET-22b-M1表达载体;IPTG诱导后高效表达出分子质量约为28 ku的M1融合蛋白;纯化的目的蛋白在SDS-PAGE图谱上呈单一条带,且获得的M1蛋白纯度达95.4%。
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| 关 键 词： | H5N1 禽流感 基质蛋白M1 原核表达 纯化 |
Prokaryotic Expression and Purification of Avian Influenza Virus (H5N1) M1 Gene |
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| CHU Jie-yuan,WANG Hai-jun,WANG Chun-yu,CHEN DI,WANG Quan-kai. Prokaryotic Expression and Purification of Avian Influenza Virus (H5N1) M1 Gene[J]. Journal of Economic Animal, 2010, 14(1): 26-29 |
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| Authors: | CHU Jie-yuan WANG Hai-jun WANG Chun-yu CHEN DI WANG Quan-kai |
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| Affiliation: | 1.College of Chinese Medicinal Materials;Jilin Agricultural University;Changchun 130118;China;2.International Cooperation and Communication Office;China |
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| Abstract: | To obtain high purity recombinant M1 protein which purity is more than 90%,the M1 gene was inserted into the pET-22b system before the constructed recombinant plasmid was transformed into BL21(DE3).The recombinant protein was expressed and identified by SDS-PAGE and then purified by Ni2+affinity chromatography and column chromatography.More than 95.4% purity recombinant M1 protein was obtained.The result showed that the relative molecular mass of expressed product was 28 000,which was consistent with that o... |
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| Keywords: | H5N1 avian influenza matrix protein M1 prokaryotic expression purification |
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