| Literature DB >> 21158445 |
Xin Huang1, Aleksey V Tolmachev, Yulei Shen, Miao Liu, Lin Huang, Zhixin Zhang, Gordon A Anderson, Richard D Smith, Wing C Chan, Steven H Hinrichs, Kai Fu, Shi-Jian Ding.
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.Entities:
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Year: 2011 PMID: 21158445 PMCID: PMC3065106 DOI: 10.1021/pr1010058
Source DB: PubMed Journal: J Proteome Res ISSN: 1535-3893 Impact factor: 4.466