乙酰化蛋白的质谱鉴定研究identification of acetylated proteins by .pdfVIP

2008 年第 66 卷 化 学 学 报 Vol. 66, 2008 第 22 期, 2563～2568 ACTA CHIMICA SINICA No. 22, 2563～2568 ·研究简报· 乙酰化蛋白的质谱鉴定研究 祝叶萍a,b 樊惠芝*,a 沈诚频a,b 姚 鋆 b 周新文b 杨芃 原*,a,b (a 复旦大学化学系 上海 200433) (b 复旦大学生物医学研究院 上海 200032) 摘要 报道了两种生物质谱技术 ESI-MS 和 MALDI-MS 在鉴定乙酰化修饰蛋白 BSA-ac 中的应用研究结果. 乙酰化修 饰蛋白通过特征碎裂峰 m/z 126.1 或 MS/MS 质谱图中相差一个赖氨酸的相邻 b 或 y 离子之间 170 Da 分子量的差异确证 赖氨酸乙酰化修 , 并且后者提供具体修饰位点信息. 研究提示 ESI-MS 和 MALDI-MS 两种质谱技术均可用于鉴定实 际复杂样品中的乙酰化蛋白, 且在乙酰化蛋白的鉴定中各有其优点. 关键词 乙酰化蛋白; 翻译后修 ; 质谱; 鉴定 Identification of Acetylated Proteins by Mass Spectrometry ZHU, Ye-Pinga,b FAN, Hui-Zhi*,a SHEN, Cheng-Pina,b YAO, Junb ZHOU, Xin-Wenb YANG, Peng-Yuan*,a,b a ( Department of Chemistry, Fudan University, Shanghai 200433) (b Institute of Biomedical Sciences, Fudan University, Shanghai 200032) Abstract Identification of acetylated proteins was performed via identifying BSA-ac by two kinds of mass spectrometers including ESI-MS and MALDI-MS. The lysine-acetylated proteins can be confirmed from the observation of a specific ion at m/z 126.1 or a mass difference of 170 Da between the adjacent b-ions or y-ions. The LTQ-Orbitrap hybrid spectrometer (ESI-MS) comprising an LC pre-concentration system and an ESI ionization source could acquire much more information than the others. However, the ion at m/z 126.1 could not be detected with a linear ion trap analyzer, which was well observed throu