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Updated: Jul 16, 2026

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
Published on: October 13, 2009
Protein phosphorylation degree: determination by capillary liquid chromatography and inductively coupled plasma mass
1Central Spectroscopy and Department of Biophysics, German Cancer Research Center (DKFZ), Heidelberg.
Abstract:
Capillary liquid chromatography (muLC) interfaced to inductively coupled plasma mass spectrometry (ICPMS) is introduced as a new micromethod to determine the phosphorylation degree in phosphoproteins and phosphopeptides containing cysteine and/or methionine residues. The stoichiometric phosphorus to sulfur (31P to 32S) ratio is experimentally determined by muLC-ICPMS and converted into the degree of phosphorylation using protein/ peptide sequence information. The method is applied to the phosphoproteins beta-casein, beta-casein, and recombinant protein kinase A catalytic subunit and to synthetic phosphopeptides. The accurate data obtained by muLC-ICPMS allow quantitative assessment of the compound-specific discrimination of the electrospray ionization process between nonphosphorylated and phosphorylated proteins and peptides.
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