Identification of phosphorylation sites in phosphopeptides by positive and negative mode electrospray ionization tandem mass spectrometry
Identification of phosphorylation sites in phosphopeptides by positive and negative mode electrospray ionization tandem mass spectrometry
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DOI：
10.1016/1044-0305(95)00675-3
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发表时间：
1996-03-01
影响因子：
3.2
通讯作者：
Knapp, DR
中科院分区：
文献类型：
--
作者：
Busman, M;Schey, KL;Knapp, DR
一系列合成的单磷酸化和二磷酸化肽已被分析的积极和消极的模式电喷雾电离串联质谱。合成肽是来自视紫红质C-末端区域的蛋白水解片段的丝氨酸-和苏氨酸-磷酸化类似物。探索了使用电喷雾电离的正模式和负模式通过低能碰撞诱导解离产生用于串联质谱的离子。对于一些肽，互补使用的实验结果允许确定的磷酸化位点时，任何一种模式单独给出不完整的信息。然而，其他肽给出了骨架裂解方面不可解释的负离子光谱。然而，使用不同电荷状态的前体离子的正离子串联质谱在大多数情况下提供了足够的信息来分配磷酸化位点。这些结果说明了通过使用不同电荷极性或数目的前体离子通过串联质谱法获得互补信息的效用。
A series of synthetic mono- and diphosphorylated peptides has been analyzed by positive and negative mode electrospray ionization-tandem mass spectrometry. The synthetic peptides are serine- and threonine-phosphorylated analogs of proteolytic fragments from the C-terminal region of rhodopsin. Use of positive and negative modes of electrospray ionization to produce ions for tandem mass spectrometry via low energy collision-induced dissociation was explored. For some of the peptides, the complementary use of experimental results allowed determination of the phosphorylation sites when either mode alone gave incomplete information. Other peptides, however, gave negative ion spectra not interpretable in terms of backbone cleavages. However, use of positive ion tandem mass spectrometry of different charge state precursor ions gave sufficient information in most eases to assign sites of phosphorylation. These results illustrate the utility of obtaining complementary information by tandem mass spectrometry by using precursor ions of different charge polarity or number.