Acta Chimica Sinica ›› 2008, Vol. 66 ›› Issue (22): 2563-2568. Previous Articles     Next Articles



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


  1. (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)

  • 投稿日期:2008-05-09 修回日期:2008-06-05 发布日期:2008-11-28
  • 通讯作者: 杨芃原

Identification of Acetylated Proteins by Mass Spectrometry

ZHU, Ye-Ping a,b FAN, Hui-Zhi *,a SHEN, Cheng-Pin a,b
YAO, Jun b ZHOU, Xin-Wen b YANG, Peng-Yuan *,a,b

  1. (a Department of Chemistry, Fudan University, Shanghai 200433)
    (b Institute of Biomedical Sciences, Fudan University, Shanghai 200032)

  • Received:2008-05-09 Revised:2008-06-05 Published:2008-11-28
  • Contact: YANG, Peng-Yuan

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 through a 4700 Proteomic analyzer (MALDI-TOF-TOF). This diagnostic ion can also reduce the false positive rate. It has been demonstrated that ESI and MALDI MS are complementary to each other in analyzing acetylated proteins. Accordingly, it can be concluded from the fact that different results would be obtained with different mass spectrometers, and matched protocols should be used for the identification of the acetylated proteins.

Key words: acetylated protein, post-translational modification, mass spectrometry, identification