Mass spectrometric analysis of protein histidine phosphorylation

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

doi:10.1007/s00726-007-0493-4

Mass spectrometric analysis of protein histidine phosphorylation

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

Research output: Contribution to journal › Article › peer-review

39 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 language	English
Pages (from-to)	347-357
Journal	Amino Acids
Volume	32
Issue number	3
DOIs	https://doi.org/10.1007/s00726-007-0493-4
Publication status	Published - 2007

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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.",

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AU - Zu, X.

AU - Besant, Paul

AU - Imhof, A.

AU - Attwood, Paul

PY - 2007

Y1 - 2007

N2 - 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.

AB - 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.

U2 - 10.1007/s00726-007-0493-4

DO - 10.1007/s00726-007-0493-4

M3 - Article

C2 - 17334905

SN - 0939-4451

VL - 32

SP - 347

EP - 357

JO - Amino Acids

JF - Amino Acids

IS - 3

ER -

Mass spectrometric analysis of protein histidine phosphorylation

Abstract

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