論文

査読有り
2016年12月

A proteomic approach for the analysis of S-nitrosylated proteins using a fluorescence labeling technique

Journal of Electrophoresis
  • Yoshimura Toshihiro
  • ,
  • Kurogi Katsuhisa
  • ,
  • Liu Ming-Cheh
  • ,
  • Suiko Masahito
  • ,
  • Sakakibara Yoichi

60
1
開始ページ
5
終了ページ
14
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.2198/jelectroph.60.5
出版者・発行元
日本電気泳動学会

<p><i>S</i>-nitrosylation, a post-translational modification of the thiol group of cysteine residues by nitric oxide (NO), has emerged as a new mode of signal transduction and regulation of protein function. It has recently been shown that <i>S</i>-nitrosylation may result in various protein dysfunctions. However, an improved <i>S</i>-nitrosylation analysis method is needed to achieve high sensitivity and quantitative accuracy. We hypothesized that an analysis method using fluorescence dye could detect <i>S</i>-nitrosylated proteins at a higher sensitivity than that of the conventional method. In this study, we developed a procedure for analyzing <i>S</i>-nitrosylated proteins using CyDye (the CyDye switch method). This CyDye switch method for detecting <i>S</i>-nitrosylated proteins was developed based on the biotin-switch method for analyzing <i>S</i>-nitrosylated proteins. We analyzed NO donor-induced <i>S</i>-nitrosylated proteins in a model protein and at the cellular level. We demonstrated that this CyDye switch method could detect specific <i>S</i>-nitrosylated proteins using SDS-PAGE and mass spectrometry. Our results indicate that the optimized CyDye switch method is suita

リンク情報
DOI
https://doi.org/10.2198/jelectroph.60.5
CiNii Articles
http://ci.nii.ac.jp/naid/130005252665
ID情報
  • DOI : 10.2198/jelectroph.60.5
  • CiNii Articles ID : 130005252665

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