論文 - 詳細
| RRC ID | 52303 |
|---|---|
| 著者 | Kubota Y, Fujioka K, Takekawa M. |
| タイトル | WGA-based lectin affinity gel electrophoresis: A novel method for the detection of O-GlcNAc-modified proteins. |
| ジャーナル | PLoS One |
| Abstract |
Post-translational modification with O-linked β-N-acetylglucosamine (O-GlcNAc) occurs selectively on serine and/or threonine residues of cytoplasmic and nuclear proteins, and dynamically regulates their molecular functions. Since conventional strategies to evaluate the O-GlcNAcylation level of a specific protein require time-consuming steps, the development of a rapid and easy method for the detection and quantification of an O-GlcNAcylated protein has been a challenging issue. Here, we describe a novel method in which O-GlcNAcylated and non-O-GlcNAcylated forms of proteins are separated by lectin affinity gel electrophoresis using wheat germ agglutinin (WGA), which primarily binds to N-acetylglucosamine residues. Electrophoresis of cell lysates through a gel containing copolymerized WGA selectively induced retardation of the mobility of O-GlcNAcylated proteins, thereby allowing the simultaneous visualization of both the O-GlcNAcylated and the unmodified forms of proteins. This method is therefore useful for the quantitative detection of O-GlcNAcylated proteins. |
| 巻・号 | 12(7) |
| ページ | e0180714 |
| 公開日 | 2017-7-7 |
| DOI | 10.1371/journal.pone.0180714 |
| PII | PONE-D-16-35933 |
| PMID | 28686627 |
| PMC | PMC5501588 |
| MeSH | Acetylglucosamine / chemistry* Acetylglucosamine / metabolism Electrophoresis Glycosylation Protein Processing, Post-Translational* Proteins / chemistry Proteins / isolation & purification Proteins / metabolism* Wheat Germ Agglutinins / chemistry |
| IF | 2.74 |
| 引用数 | 4 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
|
| 最多言及媒体 | X(Twitter) |
| 各媒体での言及数の合計 | 3 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| ヒト・動物細胞 | 293(RCB1637) COS-7(RCB0539) |