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

• Sasaki Takeshi

  Department Of Biotechnology College Of Agriculture Ehime University

• Akiyama K

  Ehime Univ. Matsuyama Jpn

• Takata R

  Ehime Univ. Matsuyama Jpn

• Takata Renkichi

  Department Of Applied Life Science Faculty Of Agriculture Ehime University

• ASDORNNITHEE SOMSIT

  Department of Biotechnology, College of Agriculture, Ehime University

• HIMEJI EIICHI

  Department of Biotechnology, College of Agriculture, Ehime University

• AKIYAMA KOUICHI

  Department of Biotechnology, College of Agriculture, Ehime University

• Himeji Eiichi

  Department Of Biotechnology College Of Agriculture Ehime University

• Asdornnithee Somsit

  Department Of Biotechnology College Of Agriculture Ehime University

• Sasaki T

  Ehime Univ. Ehime Jpn

• Sasaki Takeshi

  Department Of Agricultural Chemistry Faculty Of Agriculture Ehime University

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