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MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics.


ABSTRACT: Quantitative mass spectrometry-based proteomics is highly versatile but not easily multiplexed. Isobaric labeling strategies allow mass spectrometry-based multiplexed proteome quantification; however, ratio distortion owing to protein quantification interference is a common effect. We present a two-proteome model (mixture of human and yeast proteins) in a sixplex isobaric labeling system to fully document the interference effect, and we report that applying triple-stage mass spectrometry (MS3) almost completely eliminates interference.

SUBMITTER: Ting L 

PROVIDER: S-EPMC3205343 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature

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MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics.

Ting Lily L   Rad Ramin R   Gygi Steven P SP   Haas Wilhelm W  

Nature methods 20111002 11


Quantitative mass spectrometry-based proteomics is highly versatile but not easily multiplexed. Isobaric labeling strategies allow mass spectrometry-based multiplexed proteome quantification; however, ratio distortion owing to protein quantification interference is a common effect. We present a two-proteome model (mixture of human and yeast proteins) in a sixplex isobaric labeling system to fully document the interference effect, and we report that applying triple-stage mass spectrometry (MS3) a  ...[more]

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