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学科主题: 生命有机化学
题名: Over-expression and refolding of isotopically labeled recombinant catalytic domain of human macrophage elastase (MMP-12) for NMR studies
其他题名: 用于NMR 研究的基质金属蛋白酶MMP12催化域重组子的表达和重折叠
作者: Zheng XH(郑训海) ; Ou L(欧力) ; Tong XT(童孝田) ; Zhu J(朱静) ; Wu HM(吴厚铭)
通讯作者: 吴厚铭
刊名: Protein Expr. Purif.
发表日期: 2007
卷: 56, 期:2, 页:160-166
收录类别: SCI
部门归属: 上海有机化学研究所生命有机化学国家重点实验室
英文摘要: Human macrophage elastase (MMP-12) plays an important role in inflammatory processes and is involved in a number of physiological or pathological situations, such as conversion of plasminogen into angiotatin, allergic airway inflammation, vascular remodeling or alteration, as well as emphysema, and has been justified as a novel drug target. Here, we report the over-expression in Escherichia coil, purification and refolding of MMP-12 catalytic domain for NMR studies. The primary sequence of expressed protein was identified by means of MALDI-TOF MS, and was confirmed by the MALDI-TOF MS data of trypsin-digested peptides. A significantly optimized protocol has been worked out to prepare N-15 and/or C-13-labeled MMP-12 catalytic domain, and the yield of the purified protein is estimated to 10-12 mg from 0.5 L of M9 minimal media. Finally, the N-15-H-1 HSQC spectrum of uniformly N-15-labeled MMP-12 catalytic domain indicates the presence of well-ordered and properly folded protein in a monomeric form. (C) 2007 Elsevier Inc. All rights reserved.
语种: 英语
相关网址: 查看原文
WOS记录号: WOS:000251312300003
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内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/17383
Appears in Collections:上海有机化学研究所_期刊论文

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Recommended Citation:
Zheng XH,Ou L,Tong XT,et al. Over-expression and refolding of isotopically labeled recombinant catalytic domain of human macrophage elastase (MMP-12) for NMR studies[J]. Protein Expr. Purif.,2007,56(2):160-166.
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