2016年12月
A proteomic approach for the analysis of S-nitrosylated proteins using a fluorescence labeling technique
Journal of Electrophoresis
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- 巻
- 60
- 号
- 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
- ID情報
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- DOI : 10.2198/jelectroph.60.5
- CiNii Articles ID : 130005252665