%0 Journal Article
%T Construction of translation-coupled bicistronic expression vector and soluble expression of lumbrokinase F238 in E. coli<br>双顺反子翻译偶联表达载体的构建及蚓激酶基因F238在大肠杆菌中的可溶性表达
%A LI Ming
%A SONG Xin-Yu
%A WANG Xiao-Juan
%A LIU Jian-Jun
%A ZHANG Jian-Zhong
%A LIU Meng
%A HUANG Yun-Yan
%A <br>黎明
%A 宋馨宇
%A 王晓娟
%A 刘建军
%A 张建中
%A 刘萌
%A 黄云雁
%J 微生物学通报
%D 2011
%I 
%X In order to express soluble foreign proteins in E. coli, a bicistronic translation-coupled expression vector pDICT was constructed by using thioredoxin as a molecular chaperone. In this study, the expression vector pDICT was built by inserting thioredoxin gene into the pET22b vector between Nde I and EcoR I sites, and adding ribosome binding site before the stop codon of thioredoxin. Lumbrokinase gene F238 was cloned into this vector, and transformed into E. coli BL21(DE3), then the recombinant protein was induced by IPTG. SDS-PAGE results showed that the Lumbrokinase F238 was soluble expressed. The fibrinolytic activity was measured by using artificial fibrin plates, and the result indicated that Lumbrokinase could directly dissolve fibrous protein, and also had fibrinokinase activity which could indirectly dissolve fibrous protein. Construction of the bicistronic translation-coupled expression vector provides a new method to achieve soluble expression of heterologous proteins in E. coli.
%K Lumbrokinase
%K Molecular chaperones
%K Bicistronic
%K Soluble expression<br>蚓激酶
%K 分子伴侣
%K 双顺反子
%K 可溶性表达
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=78024727B5F4EF6AA9CA8E605B5FC464&aid=C38B24F2A5403A3C1D4952788BB2C36B&yid=9377ED8094509821&vid=16D8618C6164A3ED&iid=DF92D298D3FF1E6E&sid=0C7160AA184DEC96&eid=D7C79E0E439D0B57&journal_id=0253-2654&journal_name=微生物学通报&referenced_num=0&reference_num=14