| Literature DB >> 17334905 |
X-L Zu1, P G Besant, A Imhof, P V Attwood.
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.Entities:
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Year: 2007 PMID： 17334905 DOI： 10.1007/s00726-007-0493-4
Source DB: PubMed Journal: Amino Acids ISSN： 0939-4451 Impact factor: 3.520