Journal
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
Volume 20, Issue 12, Pages 2211-2220Publisher
SPRINGER
DOI: 10.1016/j.jasms.2009.08.009
Keywords
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Funding
- Engineering and Physical Sciences Research Council [EP/D013615/1]
- Biotechnology and Biological Sciences Research Council [BB/D013615/1]
- Royal Society
- Yorkshire Cancer Research, Cancer Research UK
- Medical Research Council
- MRC [G120/1030] Funding Source: UKRI
- Medical Research Council [G120/1030] Funding Source: researchfish
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Quantification of the stoichiometry of phosphorylation is usually achieved using a mixture of phosphatase treatment and differential isotopic labeling. Here, we introduce a new approach to the concomitant determination of absolute protein concentration and the stoichiometry of phosphorylation at predefined sites. The method exploits QconCAT to quantify levels of phosphorylated and nonphosphorylated peptide sequences in a phosphoprotein. The nonphosphorylated sequence is used to determine the absolute protein quantity and serves as a reference to calculate the extent of phosphorylation at the second peptide. Thus, the stoichiometry of phosphorylation and the absolute protein concentration can be determined accurately in a single experiment. (J Am Soc Mass Spectrom 2009, 20, 2211-2220) (C) 2009 American Society for Mass Spectrometry
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