Journal
AMINO ACIDS
Volume 32, Issue 3, Pages 347-357Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-007-0493-4
Keywords
phosphohistidine; mass spectrometry; phosphoamino acid analysis; histone H4; phosphopeptide; histidine kinase
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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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