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

スポンサーリンク

概要

• 論文の詳細を見る

• 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.

• 社団法人 日本農芸化学会の論文
• 2007-12-23

著者

• Koizumi Yukio

  Division Of Applied Life Sciences Graduate School Of Agriculture Kyoto University

• Sekiya Jiro

  Division Of Applied Life Sciences Graduate School Of Agricultural Sciences Kyoto University

• Kumada Henri-obadja

  Division Of Applied Life Sciences Graduate School Of Agriculture Kyoto University

関連論文

• Purification and Characterization of Cystine Lyase a from Broccoli Inflorescence
• Synthesis of Hydroxymethylglutathione from Glutathione and L-Serine Catalyzed by Carboxypeptidase Y(Biochemistry & Molecular Biology)
• Cloning and molecular analysis of radish (Raphanus sativus L.) cDNAs encoding heterodimeric γ-glutamyltransferases
• Subcellular Localization and Possible Functions of γ-Glutamyltransferase in the Radish (Raphanus sativus L.) Plant
• Purification and Properties of Soluble and Bound γ-Glutamyltransferases from Radish Cotyledon
• Laser Microdissection in Combination with Microarray-Based Gene Expression Analysis
• Purification and Characterization of Dipeptidase Hydrolyzing L-Cysteinylglycine from Radish Cotyledon

スポンサーリンク