Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers
Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers
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DOI：
10.1016/s0014-5793(03)00070-x
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发表时间：
2003-02-27
期刊：
影响因子：
3.5
通讯作者：
Waugh, DS
中科院分区：
文献类型：
--
作者：
Fox, JD;Routzahn, KM;Waugh, DS
大肠杆菌麦芽糖结合蛋白（MBP）经常被用作亲和标签，以促进重组蛋白的纯化。MBP的一个重要的附加属性是其增强其融合配偶体的溶解度的显著能力。MBPs存在于多种微生物中，包括嗜温和嗜热细菌和古细菌。在本研究中，我们比较了六种不同微生物（E。coli，Pyrococcus furiosus，Thermococcus litoralis，Vibrio cholesterol，Thermotoga maritima，和Yersinia pestis）中，以提高8种不同的聚集倾向蛋白在E.杆菌与谷胱甘肽S-转移酶（GST）相比，所有这些MBP都被证明是有效的增溶剂，其中一些甚至比E. coli MBP。(C)2003年由Elsevier Science B. V.代表欧洲生物化学学会联合会出版。
Escherichia coli maltose-binding protein (MBP) is frequently used as an affinity tag to facilitate the purification of recombinant proteins. An important additional attribute of MBP is its remarkable ability to enhance the solubility of its fusion partners. MBPs are present in a wide variety of microorganisms including both mesophilic and thermophilic bacteria and archaea. In the present study, we compared the ability of MBPs from six diverse microorganisms (E. coli, Pyrococcus furiosus, Thermococcus litoralis, Vibrio cholerae, Thermotoga maritima, and Yersinia pestis) to promote the solubility of eight different aggregation-prone proteins in E. coli. In contrast to glutathione S-transferase (GST), all of these MBPs proved to be effective solubility enhancers and some of them were even more potent solubilizing agents than E. coli MBP. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.