Purification and Characterization of a Major Collagenase from Streptomyces parvulus
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概要
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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.
- 社団法人 日本農芸化学会の論文
著者
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TAKAHASHI Kenji
Department of Radiological Life Sciences, Hirosaki University Graduate School of Health Sciences
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YAMAMOTO Masayuki
Department of Biochemistry, Tohoku University School of Medicine
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井上 英史
School Of Life Sciences Tokyo Univ. Of Pharmacy And Life Sciences
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TAKAHASHI Takayuki
Department of Clinical Immunology and Hematology, Kobe City General Hospital
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Inoue Hideshi
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo
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IINO Yuichi
Department of Surgery II, Gunma University Faculty of Medicine
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SAKURAI Yasuko
Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo
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NISHII Wataru
School of Life Science, Tkyo University of Pharmacy and Life aascience
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