Expression in Escherichia coli, Refolding, and Purification of the Recombinant Mature Form of Human Matrix Metalloproteinase 7 (MMP-7)
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概要
- 論文の詳細を見る
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.
- 社団法人 日本農芸化学会の論文
著者
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Kubo Motoki
Department Of Bioscience And Technology Faculty Of Science And Engineering Ritsumeikan University
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INOUYE Kuniyo
Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
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MATSUMIYA Yoshiki
Department of Bioscience and Technology, Faculty of Science and Engineering, Ritsumeikan University
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Muta Yuko
Division Of Food Science And Biotechnology Graduate School Of Agriculture Kyoto University
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YASUI Natsuki
Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
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