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UNiquant, a program for quantitative proteomics analysis using stable isotope labeling.


ABSTRACT: Stable isotope labeling (SIL) methods coupled with nanoscale liquid chromatography and high resolution tandem mass spectrometry are increasingly useful for elucidation of the proteome-wide differences between multiple biological samples. Development of more effective programs for the sensitive identification of peptide pairs and accurate measurement of the relative peptide/protein abundance are essential for quantitative proteomic analysis. We developed and evaluated the performance of a new program, termed UNiquant, for analyzing quantitative proteomics data using stable isotope labeling. UNiquant was compared with two other programs, MaxQuant and Mascot Distiller, using SILAC-labeled complex proteome mixtures having either known or unknown heavy/light ratios. For the SILAC-labeled Jeko-1 cell proteome digests with known heavy/light ratios (H/L = 1:1, 1:5, and 1:10), UNiquant quantified a similar number of peptide pairs as MaxQuant for the H/L = 1:1 and 1:5 mixtures. In addition, UNiquant quantified significantly more peptides than MaxQuant and Mascot Distiller in the H/L = 1:10 mixtures. UNiquant accurately measured relative peptide/protein abundance without the need for postmeasurement normalization of peptide ratios, which is required by the other programs.

SUBMITTER: Huang X 

PROVIDER: S-EPMC3065106 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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UNiquant, a program for quantitative proteomics analysis using stable isotope labeling.

Huang Xin X   Tolmachev Aleksey V AV   Shen Yulei Y   Liu Miao M   Huang Lin L   Zhang Zhixin Z   Anderson Gordon A GA   Smith Richard D RD   Chan Wing C WC   Hinrichs Steven H SH   Fu Kai K   Ding Shi-Jian SJ  

Journal of proteome research 20110125 3


Stable isotope labeling (SIL) methods coupled with nanoscale liquid chromatography and high resolution tandem mass spectrometry are increasingly useful for elucidation of the proteome-wide differences between multiple biological samples. Development of more effective programs for the sensitive identification of peptide pairs and accurate measurement of the relative peptide/protein abundance are essential for quantitative proteomic analysis. We developed and evaluated the performance of a new pro  ...[more]

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