title: Mass spectrometric analysis of protein histidine phosphorylation.
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.
authors.affiliation: School of Biomedical, Biomolecular and Chemical Sciences (M310), The University of Western Australia, Crawley, WA, Australia.
authors.forename: X-L
authors.initials: XL
authors.lastname: Zu
authors.forename: P G
authors.initials: PG
authors.lastname: Besant
authors.forename: A
authors.initials: A
authors.lastname: Imhof
authors.forename: P V
authors.initials: PV
authors.lastname: Attwood
mesh_terms: D000818:Animals; D002417:Cattle; D004331:Drosophila melanogaster; D006639:Histidine / Q000031:analogs & derivatives* / Q000032:analysis*; D006657:Histones / Q000032:analysis*; D010750:Phosphoproteins / Q000032:analysis*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D006657:Histones; D010750:Phosphoproteins; D006639:Histidine; C005436:phosphohistidine