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Expression Optimization and Characterization of the Catalytic Domain of Human MT3-MMP
引用本文:SHI Xiu-juan JIN Feng-hai WANG Hui-ling YANG Jin-gang WANG Zhi-yong FANG Xue-xun. Expression Optimization and Characterization of the Catalytic Domain of Human MT3-MMP[J]. 高等学校化学研究, 2006, 22(2): 129-133. DOI: 10.1016/S1005-9040(06)60061-5
作者姓名:SHI Xiu-juan JIN Feng-hai WANG Hui-ling YANG Jin-gang WANG Zhi-yong FANG Xue-xun
作者单位:SHI Xiu-juan 1,3,JIN Feng-hai 1,2,WANG Hui-ling 1,3,YANG Jin-gang 1,WANG Zhi-yong 1 and FANG Xue-xun 1**1. Key Laboratory of Molecular Enzymology and Engineering,the Ministry of Education; 2. School of Pharmacy; 3. College of Life Science,Jilin University,Changchun 130021,P. R. China
基金项目:Supported by the National Natural Science Foundation of China( No. 30371656).
摘    要:Introduction Matrixmetalloproteinases(MMPs)areafamilyof calciumandzincrequiringendoproteinasesthattogether candegradeallthemaincomponentsoftheextra cellu larmatrixandbasementmembranes[1].MMPsarein volvedinawiderangeofproteolyticevents,innormal andpatholog…

关 键 词:矩阵金属蛋白酶 蛋白质表达 催化反应 MMP-16 生物学作用
文章编号:1005-9040(2006)-02-129-05
收稿时间:2006-01-10

Expression Optimization and Characterization of the Catalytic Domain of Human MT3-MMP
Xiu-juan SHI, Feng-hai JIN, Hui-ling WANG, Jin-gang YANG, Zhi-yong WANG,Xue-xun FANG,. Expression Optimization and Characterization of the Catalytic Domain of Human MT3-MMP[J]. Chemical Research in Chinese University, 2006, 22(2): 129-133. DOI: 10.1016/S1005-9040(06)60061-5
Authors:Xiu-juan SHI   Feng-hai JIN   Hui-ling WANG   Jin-gang YANG   Zhi-yong WANG  Xue-xun FANG  
Affiliation:aKey Laboratory of Molecular Enzymology and Engineering, the Ministry of Education, Jilin University, Changchun 130021, P. R. China;bSchool of Pharmacy, Jilin University, Changchun 130021, P. R. China;cCollege of Life Science, Jilin University, Changchun 130021, P. R. China
Abstract:Matrix metalloproteinases(MMPs) are a family of proteases that are required for many biological processes and are also elevated in many pathological conditions. MMP inhibitors(MMPIs) may therefore be useful as therapeutic {agents} in treating a number of diseases including cancer, cardiovascular diseases and arthritis. Attempts have been made to develop MMPIs. Recombinant MMPs have been used to screening MMPs in vitro assays. In this work, we report the expression of MMP-16 in E. coli and the characterization of the recombinant MMP-16 with a commonly used MMP substrate DQ-gelatin.
Keywords:Matrix metalloproteinase(MMP)  Protein expression  Catalytic domain  MMP-16
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