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Title: The Use of a Quantitative Cysteinyl-peptide Enrichment Technology for High-Throughput Quantitative Proteomics

Abstract

Quantitative proteomic measurements are of significant interest in studies aimed at discovering disease biomarkers and providing new insights into biological pathways. A quantitative cysteinyl-peptide enrichment technology (QCET) can be employed to achieve higher efficiency, greater dynamic range, and higher throughput in quantitative proteomic studies that utilize stable-isotope labeling techniques combined with high-resolution liquid chromatography (LC)-mass spectrometry (MS) measurements. The QCET approach involves specific 16O/18O labeling of tryptic peptides, high-efficiency enrichment of cysteinyl-peptides, and confident protein identification and quantification from high resolution LC-Fourier transform ion cyclotron resonance mass spectrometry (FTICR) measurements and a previously established database of accurate mass and elution time information. This methodology is demonstrated by using proteome profiling of naïve and in vitro-differentiated human mammary epithelial cells (HMEC) as an example, which initially resulted in the identification and quantification of 603 proteins in a single LC-FTICR analysis. QCET provides not only highly efficient enrichment of cysteinyl-peptides for more extensive proteome coverage and improved labeling efficiency for better quantitative measurements, but more importantly, a high-throughput strategy suitable for quantitative proteome analysis where extensive or parallel proteomic measurements are required, such as in time course studies of specific pathways and clinical sample analyses for biomarker discovery.

Authors:
; ; ;
Publication Date:
Research Org.:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1006333
Report Number(s):
PNNL-SA-44833
400412000; TRN: US201105%%996
DOE Contract Number:  
AC05-76RL01830
Resource Type:
Book
Resource Relation:
Related Information: Quantitative Proteomics by Mass Spectrometry, Methods in Molecular Biology, 359:107-24
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; BIOLOGICAL PATHWAYS; CHROMATOGRAPHY; DISEASES; EFFICIENCY; ION CYCLOTRON-RESONANCE; MASS SPECTROSCOPY; PEPTIDES; PROTEINS; RESOLUTION; SPECTROSCOPY

Citation Formats

Liu, Tao, Qian, Weijun, Camp, David G, and Smith, Richard D. The Use of a Quantitative Cysteinyl-peptide Enrichment Technology for High-Throughput Quantitative Proteomics. United States: N. p., 2007. Web.
Liu, Tao, Qian, Weijun, Camp, David G, & Smith, Richard D. The Use of a Quantitative Cysteinyl-peptide Enrichment Technology for High-Throughput Quantitative Proteomics. United States.
Liu, Tao, Qian, Weijun, Camp, David G, and Smith, Richard D. 2007. "The Use of a Quantitative Cysteinyl-peptide Enrichment Technology for High-Throughput Quantitative Proteomics". United States.
@article{osti_1006333,
title = {The Use of a Quantitative Cysteinyl-peptide Enrichment Technology for High-Throughput Quantitative Proteomics},
author = {Liu, Tao and Qian, Weijun and Camp, David G and Smith, Richard D},
abstractNote = {Quantitative proteomic measurements are of significant interest in studies aimed at discovering disease biomarkers and providing new insights into biological pathways. A quantitative cysteinyl-peptide enrichment technology (QCET) can be employed to achieve higher efficiency, greater dynamic range, and higher throughput in quantitative proteomic studies that utilize stable-isotope labeling techniques combined with high-resolution liquid chromatography (LC)-mass spectrometry (MS) measurements. The QCET approach involves specific 16O/18O labeling of tryptic peptides, high-efficiency enrichment of cysteinyl-peptides, and confident protein identification and quantification from high resolution LC-Fourier transform ion cyclotron resonance mass spectrometry (FTICR) measurements and a previously established database of accurate mass and elution time information. This methodology is demonstrated by using proteome profiling of naïve and in vitro-differentiated human mammary epithelial cells (HMEC) as an example, which initially resulted in the identification and quantification of 603 proteins in a single LC-FTICR analysis. QCET provides not only highly efficient enrichment of cysteinyl-peptides for more extensive proteome coverage and improved labeling efficiency for better quantitative measurements, but more importantly, a high-throughput strategy suitable for quantitative proteome analysis where extensive or parallel proteomic measurements are required, such as in time course studies of specific pathways and clinical sample analyses for biomarker discovery.},
doi = {},
url = {https://www.osti.gov/biblio/1006333}, journal = {},
number = ,
volume = ,
place = {United States},
year = {Tue Jan 02 00:00:00 EST 2007},
month = {Tue Jan 02 00:00:00 EST 2007}
}

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