Quantitative analysis of mTRAQ-labeled proteome using full MS scans
- Quantitative analysis of mTRAQ-labeled proteome using full MS scans
- 강운범; 염정훈; 김호근; 이철주
- Quantitative analysis; mTRAQ; ICAT; MS1-based quantification; XCorr; b-type ion
- Issue Date
- Journal of proteome research
- VOL 9, NO 7, 3750-3758
- Proteomic techniques are mostly used these
days to identify proteins in a biological sample. Quantification
of the differences between two or more physiological
conditions, such as disease or no disease, has
become an increasingly challenging task in proteomics.
Mass tags introducing stable isotopes into peptides or
proteins provide means for quantification in mass spectrometry.
The mass tags are recognized by mass spectrometry
and at the same time provide quantitative
information. In the current study, we introduce mTRAQ
for the purpose of quantification by full MS scans.
Although mTRAQ reagent was initially designed for
multiple reaction monitoring, we verified the utility of
mTRAQ for MS1-based relative quantification using standard
protein mixtures and blood plasma samples. mTRAQlabeled
peptides showed better quality MS2 spectra with
increased XCorr values in a SEQUEST search output than
corresponding unlabeled peptides. The improved spectral
quality was due mostly to the enhanced matching of
b-type ions. By combining mTRAQ with ICAT and applying
them to colon cancer tissues, we identified and
quantified a total of 3,320 proteins. mTRAQ covered a
wider range of the proteome than did ICAT, and only 1053
proteins were shared by the two independent methods.
Our results suggest the usefulness of mTRAQ, alone or
in combination with ICAT, as a comparative profiling
method in quantitative proteomics.
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