Purification and characterization of mannose isomerase from Agrobacterium radiobacter M-I

• HIROSE Jun

  Department of Applied Chemistry, Faculty of Engineering, Miyazaki University

• MAEDA Kazuhiko

  Department of Applied Chemistry, Faculty of Engineering, Miyazaki University

• YOKOI Haruhiko

  Department of Applied Chemistry, Faculty of Engineering, Miyazaki University

• TAKASAKI Yoshiyuki

  Department of Applied Chemistry, Faculty of Engineering, Miyazaki University

書誌事項

タイトル別名

• Purification and Characterization of Mannose Isomerase from Agrobacterium radiobacter M-1.

抄録

A mannose isomerase from Agrobacterium radiobacter M-1 (formerly Pseudomonas sp. MI) was purified to electrophoretic homogeneity and characterized. A cell-free extract was separated by ammonium sulfate fractionation, Butyl-Toyopearl 650M, DEAE-Sepharose and hydroxylapatite column chromatography. Its molecular mass was estimated to be 44 kDa by SDS-PAGE and 90 kDa by gel filtration, in which the enzyme is most likely a dimer composed of two identical subunits. The purified enzyme had an optimum pH at 8.0, an optimum temperature at 60°C, a pI of 5.2 and a K_m of 20 mM, and specifically converted D-mannose and D-lyxose to ketose. The N-terminal amino acid sequence was identified.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 65 (3), 658-661, 2001

  公益社団法人 日本農芸化学会

キーワード

• D-mannose
• mannose isomerase
• Agrobacterium radiobacter
• purification

詳細情報

• CRID: 1390282681450495104
• NII論文ID: 110002680319
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.65.658
• COI: 1:CAS:528:DC%2BD3MXisFKqu7w%3D
• ISSN: 13476947
• ISSN: 09168451
• NDL書誌ID: 5738077
• PubMed: 11330684
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I5738077
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.65.658
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可