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Stepchild phosphohistidine: acid-labile phosphorylation becomes accessible by functional proteomics

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Abstract

Bioanalytical techniques were preferentially developed for the investigation of phosphohydroxyamino acids in the past and there is a wealth of information on the detection of serine, threonine and tyrosine phosphorylation in functional proteomics. However, similarly important for protein regulation and signalling is the phosphorylation of other amino acids such as histidine, but its detection is hampered by the sensitivity to acid. Mass spectrometry in conjunction with chromatographic methods is allowing us to start to get a handle on phoshohistidine. 32P-labelling and amino acid analysis for phosphorylation site determination is increasingly complemented by typical proteomic approaches based on reversed-phase peptide separation and gas-phase fragmentation. Chemical phosphorylation of peptides is a valuable tool, therefore, for the generation of analytical standards for use in method development.

RP-UPLC/Q-TOF MS/MS analysis of histidine-phosphorylated angiotensin II

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Abbreviations

CID:

collision-induced dissociation

HPLC:

high-performance liquid chromatography

LC:

liquid chromatography

MS:

mass spectrometry

MS/MS:

tandem mass spectroemtry

pHis:

phosphohistidine

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Acknowledgement

S.K. is highly indebted to Prof. Susanne Klumpp (died 17 June 2009), who guided her into the field of histidine phosphorylation in a joint project investigating the interaction of ATP with growth factors.

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Authors and Affiliations

  1. Integrierte Funktionelle Genomik, Interdisziplinäres Zentrum für Klinische Forschung, Westfälische Wilhelms-Universität Münster, Roentgenstraße 21, 48149, Münster, Germany

    Ulli Martin Hohenester & Simone König

  2. Institut für Pharmazeutische und Medizinische Chemie, Westfälische Wilhelms-Universität Münster, Roentgenstraße 21, 48149, Münster, Germany

    Katrin Ludwig & Josef Krieglstein

Authors
  1. Ulli Martin Hohenester
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  2. Katrin Ludwig
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  3. Josef Krieglstein
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  4. Simone König
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Correspondence to Simone König.

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Hohenester, U.M., Ludwig, K., Krieglstein, J. et al. Stepchild phosphohistidine: acid-labile phosphorylation becomes accessible by functional proteomics. Anal Bioanal Chem 397, 3209–3212 (2010). https://doi.org/10.1007/s00216-009-3372-x

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  • DOI: https://doi.org/10.1007/s00216-009-3372-x

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