Journal
MASS SPECTROMETRY REVIEWS
Volume 26, Issue 1, Pages 121-136Publisher
WILEY
DOI: 10.1002/mas.20116
Keywords
O-18-labeling; quantitative proteomics; comparative proteomics; mass spectrometry; oxygen-18; carboxyl oxygen exchange reaction
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Funding
- NCRR NIH HHS [RR017699, RR016741] Funding Source: Medline
- NEI NIH HHS [EY014020] Funding Source: Medline
- NATIONAL CENTER FOR RESEARCH RESOURCES [P20RR017699] Funding Source: NIH RePORTER
- NATIONAL EYE INSTITUTE [R03EY014020] Funding Source: NIH RePORTER
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A number of proteomic techniques have been developed to quantify proteins in biological systems. This review focuses on the quantitative proteomic technique known as proteolytic O-18-labeling. This technique utilizes a protease and (H2O)-O-18 to produce labeled peptides, with subsequent chromatographic and mass spectrometric analysis to identify and quantify (relative) the proteins from which the peptides originated. The technique determines the ratio of individual protein's expression level between two samples relative to each other and can be used to quantitatively examine protein expression (comparative proteomics) and post-translational modifications, and to study protein-protein interactions. The present review discusses various aspects of the O-18-labeling technique, including: its history, the advantages and disadvantages of the proteolytic O-18-labeling technique compared to other techniques, enzymatic considerations, the problem of variable incorporation of O-18 atoms into peptides with a discussion on recent advancements of the technique to overcome it, computational tools to interpret the data, and a review of the biological applications. (c) 2006 Wiley Periodicals, Inc.
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