ポスター発表
- 第2日 5月12日（火） P会場（1008/09）
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2P-23 PDF
配位子交換クロマトグラフィーを利用したチロシンリン酸化プロテオーム解析
Recent advances in MS-based proteomics coupled with specific enrichment methods for phosphopeptides allow the identification of thousands of phosphorylated sites on S, T and Y from complex biological samples. Since the content of pY is generally much lower than that of pS and pT, the identification of pY-containing peptides remains challenging even when the phosphopeptide enrichment works quite efficiently. To overcome this problem, therefore, we investigated a novel enrichment method for pY-peptides based on the interactions between pY-peptides and metal ions. We systematically evaluated various metal ions by using synthetic pY- or pS-peptides. As a result, Cu2+-immobilized column showed the highest selectivity for pY-peptides (pY/pS = 8 on average). We applied this approach to HeLa cells treated with pervanadate and found that this approach identified more pY peptides than the conventional approach.