Mass spectrometric analysis of protein histidine phosphorylation.
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.
Zu
X-L
XL
School of Biomedical, Biomolecular and Chemical Sciences (M310), The University of Western Australia, Crawley, WA, Australia.
Besant
P G
PG
Imhof
A
A
Attwood
P V
PV
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
D006657:Histones; D010750:Phosphoproteins; D006639:Histidine; C005436:phosphohistidine