Mass spectrometry-based absolute protein quantification: PSAQ™ strategy makes use of "noncanonical" proteotypic peptides

Proteomics
Michel JaquinodChristophe Bruley

Abstract

Absolute quantification of proteins using isotope dilution mass spectrometry requires the selection of proteotypic peptides. When choosing these peptides, a certain number of rules must be respected. Several of these were established to safeguard against quantification errors resulting from the isotopically labeled standard peptides not behaving in the same way as the peptides to be quantified. Of all absolute quantification methods using isotope dilution, Protein Standard for Absolute Quantification (PSAQ(TM) ) offers the maximal protein sequence coverage. In the present study, we show that the PSAQ method presents a previously unreported advantage for protein quantification as it makes use of Met/Cys-containing peptides and peptides-containing miscleavages in addition to proteotypic peptides. By increasing the total number of peptides that can be considered, robustness of quantification is improved, paving the way for a facilitated quantification of low abundant and/or low-molecular-weight proteins.

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Citations

Feb 12, 2013·Progress in Retinal and Eye Research·Gülgün Tezel
Dec 30, 2014·Proteomics·Ingo WohlgemuthHenning Urlaub
Sep 29, 2012·Journal of Mass Spectrometry : JMS·Guillaume PicardVirginie Brun
Jul 22, 2014·Proteomics·Siri HildonenLéon Reubsaet
Nov 5, 2016·Expert Opinion on Drug Discovery·Rumin Zhang, Kenny Wong
Feb 27, 2016·Mass Spectrometry Reviews·Wolf D Lehmann
Aug 11, 2012·Bioanalysis·Stephen W HolmanClaire E Eyers
Dec 17, 2014·Journal of Proteome Research·Dorothée LebertVirginie Brun

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