Huang X, Tolmachev AV, Shen Y, Liu M, Huang L, Zhang Z, Anderson GA, Smith RD, Chan WC, Hinrichs SH, Fu K, Ding SJ.
J Proteome Res. 2011 Mar 4;10(3):1228-37.
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.
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3065106/pdf/nihms268093.pdfDepartment of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska 68198, USA.
United States
