Determination of protein phosphorylation sites by mass spectrometry: a novel electrospray‐based method | Zendy

Alverdi Vera | Zendy; Di Pancrazio Francesca | Zendy; Lippe Giovanna | Zendy; Pucillo Carlo | Zendy; Casetta Bruno | Zendy; Esposito Gennaro | Zendy

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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.

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