Isolation and Characterization of Pz-Peptidase from Bacillus licheniformis N22
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概要
- 論文の詳細を見る
Pz-peptidase in an endopeptidase that cleaves the synthetic substrate, 4-phentlazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg (Pz-peptide), which was originally developed for the assay of Clostridium histolyticum collagenase (Wunsch and Heidrich, Hoppe-Seyler's Z. Physiol. Chem., 333,149-151,1963; Morales and Woessner, J. Biol. Chem., 252,4855-4860,1977). Pz-peptidase was purified from the culture filtrate of Bacillus licheniformis N22. The purified Pz-peptidase showed a molecular weight of 70,000 in SDS-polyacryl-amide gel electrophoresis and 150,000 in gel filtration. Optimal pH for cleavage of Pz-peptide was 7.8. The Pz-peptidase activity was strongly inhibited by metal chelators such as EDTA and O-phenauthroline. Substrate specificity studies indicated that Pz-peptidase cleaved oligopeptides at the Xaa-Gly site in Xaa-Gly-Pro. However, Pz-peptidase failed to hydrolyze native collagen, denatured collagen, hemoglobin and casein.
- 公益社団法人日本生物工学会の論文
- 1995-03-25
著者
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Sasaki Takeshi
Department Of Biotechnology College Of Agriculture Ehime University
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Akiyama K
Ehime Univ. Matsuyama Jpn
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Takata R
Ehime Univ. Matsuyama Jpn
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Takata Renkichi
Department Of Applied Life Science Faculty Of Agriculture Ehime University
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ASDORNNITHEE SOMSIT
Department of Biotechnology, College of Agriculture, Ehime University
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HIMEJI EIICHI
Department of Biotechnology, College of Agriculture, Ehime University
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AKIYAMA KOUICHI
Department of Biotechnology, College of Agriculture, Ehime University
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Himeji Eiichi
Department Of Biotechnology College Of Agriculture Ehime University
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Asdornnithee Somsit
Department Of Biotechnology College Of Agriculture Ehime University
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Sasaki T
Ehime Univ. Ehime Jpn
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Sasaki Takeshi
Department Of Agricultural Chemistry Faculty Of Agriculture Ehime University
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