A Combination of Unnatural Phosphatidyl Acceptor and Tandem Electrospray Ionization Mass Spectrometry for Tracing Phospholipase D Activity

DOI Web Site Web Site 被引用文献1件 参考文献41件
  • ODA Keiichi
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University Ikeda Tohka Industries Co., Ltd.
  • IMURA Megumi
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
  • UEDA Yoshimi
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
  • HOSOKAWA Miho
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
  • KOBAYASHI Michiyo
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
  • MATSUBARA Junko
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
  • SATO Mizuho
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
  • KUMURA Naokazu
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
  • IZUMI Minoru
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
  • NAKAJIMA Shuhei
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
  • SUGIO Tsuyoshi
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University
  • BABA Naomichi
    Division of Bioscience, Graduate School of Natural Science and Technology, Okayama University

この論文をさがす

抄録

Phospholipase D (PLD) is a biocatalyst in the synthesis of bioactive compounds and a key enzyme in a variety of biological signal transductions. A combination of unnatural phosphatidyl acceptor, N,N,N-triethyl-N-2-hydroxyethylammonium bromide 6, as a substrate for PLD, and tandem electrospray ionization mass spectrometry (ESI MS) was found to provide information as to whether a given phospholipid serves as a substrate for the PLD-catalyzed reaction. Thus 2-(13′-hydroperoxy-octadecadienoyl)-1-palmitoylglycerophosphocholine 1, and its degradation products 2-(13′-oxo-octadecadienoyl)-1-palmitoylglycerophosphocholine 9 and 2-(13′-hydroxy-octadecadienoyl)-1-palmitoylglycerophosphocholine 11, in a mixture were found to be a substrate of the PLD-catalyzed transphosphatidylation. The sensitivity of this method was exemplified by the observation that PLD activity in cabbage leaves was detected using a small amount of crude crushed leaves with little pretreatment. This simple method can be used in screening for PLD activity and searching for inhibitors of the enzyme from various natural sources.

収録刊行物

被引用文献 (1)*注記

もっと見る

参考文献 (41)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ