Purification and Characterization of a Major Collagenase from Streptomyces parvulus
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- SAKURAI Yasuko
- Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo
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- INOUE Hideshi
- Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo School of Life Sciences, Tokyo University of Pharmacy and Life Sciences
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- NISHII Wataru
- School of Life Sciences, Tokyo University of Pharmacy and Life Sciences
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- TAKAHASHI Takayuki
- Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo
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- IINO Yuichi
- Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo
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- YAMAMOTO Masayuki
- Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo
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- TAKAHASHI Kenji
- Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo School of Life Sciences, Tokyo University of Pharmacy and Life Sciences
Bibliographic Information
- Other Title
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- Purification and Characterization of a Major Collagenase from<i>Streptomyces parvulus</i>
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Description
A major collagenase was purified about 96-fold from a crude enzyme sample of Streptomyces parvulus by chromatography on Q-Sepharose, Sephacryl S-200, and butyl-Toyopearl. The purified enzyme showed a relative molecular mass of approximately 52,000 on SDS–PAGE and a pH optimum at about 9.0, and was strongly inhibited by metal-chelating agents. It also cleaved 4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg specifically at the Leu-Gly bond, with a Km value of 0.60 mM at pH 9.0 at 37 °C. Based on the amino acid sequences of the N-terminal region and internal tryptic peptides, the corresponding gene was cloned. The DNA sequence of the cloned gene indicated that the enzyme is produced as an 864-residue precursor protein with a 408-residue prepro sequence followed by a 456-residue mature enzyme moiety. The enzyme is most homologous with the collagenase from S. coelicolor, the identity being 73%, and it is thought to be a member of the Vibrio collagenase subfamily.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 73 (1), 21-28, 2009
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Details 詳細情報について
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- CRID
- 1390001206480215680
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- NII Article ID
- 10027535692
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- NII Book ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 9782156
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed