CRCU

Chemical Research in Chinese Universities ›› 2006, Vol. 22 ›› Issue (2): 129-133.

• Articles • Previous Articles     Next Articles

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

SHI Xiu-juan1,3, JIN Feng-hai1,2, WANG Hui-ling1,3, YANG Jin-gang1, WANG Zhi-yong1, FANG Xue-xun1   

  1. 1. Key Laboratory of Molecular Enzymology and Engineering, the Ministry of Education, Jilin University, Changchun 130021, P.R.China;

    2. School of Pharmacy, Jilin University, Changchun 130021, P.R.China;
    3. College of Life Science, Jilin University, Changchun 130021,P.R.China
  • Received:2006-01-10 Online:2006-04-24 Published:2011-08-06
  • Supported by:

    Supported by the National Natural Science Foundation of China(No.30371656).

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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.

Key words: Matrix metalloproteinase(MMP), Protein expression, Catalytic domain, MMP-16