| 外源蛋白在大肠杆菌中的折叠 |
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| 引用本文： | 康铁军,袁旭东,俞炜源. 外源蛋白在大肠杆菌中的折叠[J]. 军事医学科学院院刊, 2002, 26(4): 304-307 |
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| 作者姓名： | 康铁军 袁旭东 俞炜源 |
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| 作者单位： | 1. 军事医学科学院生物工程研究所,北京,100071
2. 沈阳空军司令部门诊部,沈阳,110015 |
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| 摘 要： | 大肠杆菌是表达外源基因最常用的宿主之一。它结构简单 ,遗传背景清楚 ,基因表达调控机制相对明确。随着对分子伴侣和折叠酶研究的深入 ,蛋白在大肠杆菌内的折叠机制逐渐为人们所认识。外源蛋白在大肠杆菌内的可溶性表达问题也逐步得到解决
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| 关 键 词： | 蛋白折叠 分子伴侣 Dsb 二硫键 可溶性表达 |
| 文章编号： | 1000-5501(2002)04-0304-04 |
| 修稿时间： | 2002-02-01 |
Heterologous proteins folding in Escherichia coli |
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| KANG Tie_Jun ,YUAN Xu_Dong ,YU Wei_Yuan. Heterologous proteins folding in Escherichia coli[J]. Bulletin of the Academy of Military Medical Sciences, 2002, 26(4): 304-307 |
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| Authors: | KANG Tie_Jun YUAN Xu_Dong YU Wei_Yuan |
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| Affiliation: | KANG Tie_Jun 1,YUAN Xu_Dong 2,YU Wei_Yuan 1 |
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| Abstract: | Escherichia coli is one of the most widely used hosts for the production of heterologous proteins and its genetics is far better characterized than those of any other microorganism. The contribution of the chaperone systems and the folding catalysts to cellular protein folding has been clarified by a number of recent papers. Recent progress in the fundamental understanding of protein folding in E.coli , together with serendipitous discoveries of soluble expression of complex eukaryotic proteins are making this bacterium more valuable than ever. |
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| Keywords: | protein folding chaperone Dsb disulfide bonds soluble expression |
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