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Mass spectrometric analysis of protein histidine phosphorylation |
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| Authors: | X.-L. Zu P. G. Besant A. Imhof P. V. Attwood |
| Affiliation: | (1) School of Biomedical, Biomolecular and Chemical Sciences (M310), The University of Western Australia, Crawley, WA, Australia;(2) Department of Molecular Biology, Adolf-Butenandt Institute, Histone Modifications Group, Ludwig-Maximilians-University of Munich, Munich, Germany |
| Abstract: | Summary. 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. |
| Keywords: | : Phosphohistidine – Mass spectrometry – Phosphoamino acid analysis – Histone H4 – Phosphopeptide – Histidine kinase |
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