Mass spectrometric analysis of protein histidine phosphorylation

@article{Zu2007MassSA,
  title={Mass spectrometric analysis of protein histidine phosphorylation},
  author={X. L. Zu and Paul G. Besant and A. Imhof and Paul V. Attwood},
  journal={Amino Acids},
  year={2007},
  volume={32},
  pages={347-357}
}
Protein histidine phosphorylation is now recognized as an important form of post-translational modification. The acid-lability of phosphohistidine has meant that this phosphorylation has not been as well studied as serine/threonine or tyrosine phosphorylation. We show that phosphohistidine and phosphohistidine-containing phosphopeptides derived from proteolytic digestion of phosphohistone H4 are detectable by ESI-MS. We also demonstrate reverse-phase HPLC separation of these phosphopeptides and… CONTINUE READING
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