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Mass spectrometric analysis of protein histidine phosphorylation

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Summary.

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 their detection by MALDI-TOF-MS.

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Zu, XL., Besant, P., Imhof, A. et al. Mass spectrometric analysis of protein histidine phosphorylation. Amino Acids 32, 347–357 (2007). https://doi.org/10.1007/s00726-007-0493-4

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