文献类型：期刊文献

中文题名：S-腺苷甲硫氨酸合成酶的可溶性表达

英文题名：Soluble Expression of S-Adenosylmethionine Synthetase

作者：陶冶[1];周佳佳[1];张书翠[1];付水林[1];宫衡[1]

机构：[1]华东理工大学生物反应器工程国家重点实验室,上海200237

年份：2012

卷号：38

期号：5

起止页码：594

中文期刊名：华东理工大学学报（自然科学版）

外文期刊名：Journal of East China University of Science and Technology

收录：CSTPCD;;Scopus;北大核心:【北大核心2011】；CSCD:【CSCD2011_2012】；

语种：中文

中文关键词：S-腺苷甲硫氨酸合成酶;pET质粒;宿主菌;可溶性;比活力

外文关键词：S-adenosylmethionine synthetase; pET plasmid; host strain; solubility; specific activity

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pET-44a为载体,trxB和gor双突变的Ori-gami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60.9U/mg。
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.