Journal
JOURNAL OF PROTEOME RESEARCH
Volume 7, Issue 1, Pages 367-374Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr070476i
Keywords
glycomics; isobaric labeling; stable isotope labeling; quantitation
Categories
Funding
- NCRR NIH HHS [P41 RR005351, P41 RR018502] Funding Source: Medline
- NATIONAL CENTER FOR RESEARCH RESOURCES [P41RR005351, P41RR018502] Funding Source: NIH RePORTER
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The study of glycosylation patterns (glycomics) in biological samples is an emerging field that can provide key insights into cell development and pathology. A current challenge in the field of glycomics is to determine how to quantify changes in glycan expression between different cells, tissues, or biological fluids. Here we describe a novel strategy, quantitation by isobaric labeling (QUIBL), to facilitate comparative glycomics. Permethylation of a glycan with (CH3I)-C-13 or (CH2DI)-C-12 generates a pair of isobaric derivatives, which have the same nominal mass. However, each methylation site introduces a mass difference of 0.002922 Da. As glycans have multiple methylation sites, the total mass difference for the isobaric pair allows separation and quantitation at a resolution of similar to 30000 m/Delta m. N-Linked oligosaccharides from a standard glycoprotein and human serum were used to demonstrate that QUIBL facilitates relative quantitation over a linear dynamic range of 2 orders of magnitude and permits the relative quantitation of isomeric glycans. We applied QUIBL to quantitate glycomic changes associated with the differentiation of murine embryonic stem cells to embryoid bodies.
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