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Determination of protein phosphorylation sites by mass spectrometry: a novel electrospray‐based method
Author(s) -
Alverdi Vera,
Di Pancrazio Francesca,
Lippe Giovanna,
Pucillo Carlo,
Casetta Bruno,
Esposito Gennaro
Publication year - 2005
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.2198
Subject(s) - chemistry , mass spectrometry , electrospray , chromatography , electrospray mass spectrometry , tandem mass spectrometry , phosphorylation , protein mass spectrometry , protein phosphorylation , phosphopeptide , sample preparation in mass spectrometry , electrospray ionization , biochemistry , protein kinase a
Several methods are used to identify protein phosphorylation sites. We report a novel electrospray‐based method for the determination of phosphorylation sites by mass spectrometry, using two different declustering potential values. This method allows one to obtain, with a single liquid chromatography/mass spectrometry (LC/MS) run, the pattern with either the phosphorylated or the unphosphorylated species of a protein tryptic digest, that can be further analyzed by tracing back the origin of each HPO 3 ‐deprived form using the capabilities of tandem mass spectrometers. Copyright © 2005 John Wiley & Sons, Ltd.