High throughput comparative proteome analysis using a quantitative cysteinyl-peptide enrichment technology
A new quantitative cysteinyl-peptide enrichment technology (QCET) was developed to achieve higher efficiency, greater dynamic range, and higher throughput in quantitative proteomics that use stable-isotope labeling techniques combined with high resolution liquid chromatography (LC)-mass spectrometry (MS). This approach involves {sup 18}O labeling of tryptic peptides, high efficiency enrichment of cysteine-containing peptides, and confident protein identification and quantification using the accurate mass and time tag strategy. Proteome profiling of naive and in vitro-differentiated human mammary epithelial cells using QCET resulted in the identification and quantification of 603 proteins in a single LC-Fourier transform ion cyclotron resonance MS analysis. Advantages of this technology include: (1) a simple, highly efficient method for enriching cysteinyl-peptides; (2) a high throughput strategy suitable for extensive proteome analysis; and (3) improved labeling efficiency for better quantitative measurements. This technology enhances both the functional analysis of biological systems and the detection of potential clinical biomarkers.
- Research Organization:
- Pacific Northwest National Lab., Richland, WA (US), Environmental Molecular Sciences Laboratory (US)
- Sponsoring Organization:
- US Department of Energy (US)
- DOE Contract Number:
- AC05-76RL01830
- OSTI ID:
- 15016091
- Report Number(s):
- PNWD-SA-6477; 10198; TRN: US200509%%915
- Journal Information:
- Analytical Chemistry, Vol. 76, Issue 18; Other Information: PBD: 15 Sep 2004
- Country of Publication:
- United States
- Language:
- English
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