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Submitted on September 16, 2004
Advanced Research and Technology, Applied Biosystems, Framingham, MA 01701
Corresponding Author: rosspl{at}appliedbiosystems.com
We describe here a multiplexed protein quantitation strategy that provides relative and absolute measurements of proteins in complex mixtures. At the core of this methodology is a multiplexed set of isobaric reagents that yield amine-derivatized peptides. The derivatized peptides are indistinguishable in MS, but exhibit intense low-mass MS/MS signature ions that support quantitation. In this study, we have examined the global protein expression of a wild-type yeast strain 2 isogenic mutant strains that are defective in the nonsense-mediated mRNA decay and the general 5’ to 3’ decay pathways by deletion of the upf1 and xrn1 genes, respectively. We also demonstrate the use of four-fold multiplexing to enable relative protein measurements simultaneously with determination of absolute levels of a target protein using synthetic isobaric peptide standards.
Revised on September 22, 2004
Accepted on September 22, 2004
Multiplexed protein quantitation in saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
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