Expression in Escherichia coli, Refolding, and Purification of the Recombinant Mature Form of Human Matrix Metalloproteinase 7 (MMP-7)

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  • MUTA Yuko
    Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
  • YASUI Natsuki
    Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
  • MATSUMIYA Yoshiki
    Department of Biotechnology, College of Life Sciences, Ritsumeikan University
  • KUBO Motoki
    Department of Biotechnology, College of Life Sciences, Ritsumeikan University
  • INOUYE Kuniyo
    Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

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  • Expression in<i>Escherichia coli</i>, Refolding, and Purification of the Recombinant Mature Form of Human Matrix Metalloproteinase 7 (MMP-7)

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In the latent pro-form of matrix metalloproteinase 7 (MMP-7), the cysteine residue in the pro-peptide binds the active-site zinc ion. Hence, recombinant active MMP-7 was prepared from pro-MMP-7 by modification of this cysteine residue with a mercuric reagent. In this study, mature MMP-7 was expressed in Escherichia coli as inclusion bodies, solubilized, and refolded with 1 M L-arginine. The purified product was indistinguishable from the one prepared from pro-MMP-7 as assessed by hydrolysis of (7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2.

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