Fragmentation of phosphopeptides in an ion trap mass spectrometer
Fragmentation of phosphopeptides in an ion trap mass spectrometer
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DOI:
10.1016/s1044-0305(98)00088-9
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发表时间:
1998-11-01
影响因子:
3.2
通讯作者:
Qin, J
中科院分区:
文献类型:
--
作者:
DeGnore, JP;Qin, J
A systematic study of the fragmentation pattern of phosphopeptides in an electrospray (ESI) ion trap mass spectrometer is presented. We show that phosphotyrosine- and phosphothreonine-containing peptides show complicated fragmentation patterns. These phosphopeptides were observed to lose the phosphate moiety in the form of H3PO4 and/or HPO3, but were also detected with no loss of the phosphate group. The tendency to lose the phosphate moiety depends strongly on the charge state. Thus, the highest observed charge state tends to retain the phosphate moiety with extensive fragmentation along the peptide backbone. We also show that phosphoserine-containing peptides have relatively simple fragmentation patterns of losing H3PO4. This loss is independent of the charge state. We suggest strategies for the accurate identification of phosphorylation sites using the ion trap mass spectrometer. (J Am Soc Mass Spectrom 1998, 9, 1175-1188) (C) 1998 American Society for Mass Spectrometry.