| S-腺苷甲硫氨酸合成酶的可溶性表达 |
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| 引用本文： | 陶冶,周佳佳,张书翠,付水林,宫衡.S-腺苷甲硫氨酸合成酶的可溶性表达[J].医学教育探索,2012(5):594-598. |
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| 作者姓名： | 陶冶 周佳佳 张书翠 付水林 宫衡 |
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| 作者单位： | 华东理工大学生物反应器工程国家重点实验室，上海 200237;华东理工大学生物反应器工程国家重点实验室，上海 200237;华东理工大学生物反应器工程国家重点实验室，上海 200237;华东理工大学生物反应器工程国家重点实验室，上海 200237;华东理工大学生物反应器工程国家重点实验室，上海 200237 |
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| 摘 要： | 系统考察了pET可溶性表达系统对酵母来源的S腺苷甲硫氨酸(SAM)合成酶基因的表达情况，结果显示：当采用含Nus·Tag融合标签的pET44a为载体，trxB和gor双突变的Origami为宿主时最适合目的蛋白的可溶性表达。进一步考察不同来源（大肠杆菌、枯草芽孢杆菌、苏云金芽孢杆菌）SAM合成酶的可溶性时，也得到了相似的结论；比较发现酵母来源的SAM合成酶可溶性表达的比活力最高达60.9 U/mg。
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| 关 键 词： | S-腺苷甲硫氨酸合成酶 pET质粒 宿主菌 可溶性 比活力 |
Soluble Expression of S-Adenosylmethionine Synthetase |
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| TAO Ye,ZHOU Jia-ji,ZHANG Shu-cui,FU Shui-lin and GONG Heng.Soluble Expression of S-Adenosylmethionine Synthetase[J].Researches in Medical Education,2012(5):594-598. |
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| Authors: | TAO Ye ZHOU Jia-ji ZHANG Shu-cui FU Shui-lin and GONG Heng |
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| Institution: | State Key Laboratory of Bioreactor Engineering, East China University of
Science and Technology, Shanghai 200237, China;State Key Laboratory of Bioreactor Engineering, East China University of
Science and Technology, Shanghai 200237, China;State Key Laboratory of Bioreactor Engineering, East China University of
Science and Technology, Shanghai 200237, China;State Key Laboratory of Bioreactor Engineering, East China University of
Science and Technology, Shanghai 200237, China;State Key Laboratory of Bioreactor Engineering, East China University of
Science and Technology, Shanghai 200237, China |
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| Abstract: | This paper systematically investigated the expression of S adenosylmethionine synthetase gene from yeast by using the pET soluble expression system. It was indicated that pET 44a (Nus fusion tag ) as the carrier and Origami (trxB and gor double mutant) as the host were suitable for the soluble expression of the target protein. Furthermore, the same result was obtained when the soluble expression of S adenosylmethionine synthetase gene from different sources (E. coli, Bacillus subtilis, Bacillus thuringiensiss) were tested. It was also found that the gene from yeast got the highest soluble expression, which the specific activity of SAM synthetase was up to 60.9 U/mg. |
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| Keywords: | S-adenosylmethionine synthetase pET plasmid host strain solubility specific activity |
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