Purification and Characterization of Dipeptidase Hydrolyzing<scp>L</scp>-Cysteinylglycine from Radish Cotyledon

• KUMADA Henri-Obadja

  Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University

• KOIZUMI Yukio

  Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University

• SEKIYA Jiro

  Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University

書誌事項

タイトル別名

• Purification and Characterization of Dipeptidase Hydrolyzing L-Cysteinylglycine from Radish Cotyledon

抄録

Dipeptidase activity was detected in the soluble fraction of radish (Raphanus sativus L.) cotyledon, and the purified enzyme had a specific activity of 7.32 nkat/mg protein for hydrolyzing L-cysteinylglycine. The dipeptidase was found to be a hexameric metalloenzyme, composed of homological 55 kDa-subunits. This is the first glutathione catabolism-related dipeptidase isolated from higher plants.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 71 (12), 3102-3104, 2007

  公益社団法人 日本農芸化学会

キーワード

• <small>L</small>-cysteinylglycine
• dipeptidase
• glutathione catabolism
• radish
• <I>Raphanus sativus</I> L.

詳細情報

• CRID: 1390001206478055424
• NII論文ID: 10027522516
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.70443
• ISSN: 13476947
• ISSN: 09168451
• NDL書誌ID: 9327301
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I9327301
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.70443
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可