Expression Optimization and Characterization of the Catalytic Domain of Human MT3-MMP

作     者：SHI Xiu-juan JIN Feng-hai WANG Hui-ling YANG Jin-gang WANG Zhi-yong FANG Xue-xun 

作者机构：Key Laboratory of Molecular Enzymology and Engineering the Ministry of Education School of Pharmacy College of Life Science Jilin University Changchun 130021 P. R. China 

出 版 物：《Chemical Research in Chinese Universities》 (高等学校化学研究（英文版）)

年 卷 期：2006年第22卷第2期

页      面：129-133页

核心收录：

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 

基　　金：SupportedbytheNationalNaturalScienceFoundationofChina(No.30371656) 

主　　题：Matrix metalloproteinase(MMP) Protein expression Catalytic domain MMP-16 

摘      要：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.