Mass spectrometric analysis of protein histidine phosphorylation

X. Zu, Paul Besant, A. Imhof, Paul Attwood

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)347-357
JournalAmino Acids
Volume32
Issue number3
DOIs
Publication statusPublished - 2007

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