Journal
MASS SPECTROMETRY REVIEWS
Volume 28, Issue 2, Pages 207-222Publisher
WILEY
DOI: 10.1002/mas.20196
Keywords
glycans; capillary electrophoresis; CE-MS
Categories
Funding
- National Institute of General Medical Sciences [GM24349]
- U.S. Department of Health and Human Services
- NIH/NCRR
- National Center for Glycomics and Glycoproteomics [RR018942]
- NATIONAL CENTER FOR RESEARCH RESOURCES [P41RR018942] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM024349] Funding Source: NIH RePORTER
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The occurrence of multiple glycosylation sites on a protein, together with the number of glycan structures which could potentially be associated with each site (microheterogeneity) often leads to a large number of structural combinations. These structural variations increase with the molecular size of a protein, thus contributing to the complexity of glycosylation patterns. Resolving such fine structural differences has been instrumentally difficult. The degree of glycoprotein micro-heterogeneity has been analytically challenging in the identification of unique glycan structures that can be crucial to a distinct biological,function. Despite the wealth of information provided by the most powerful mass spectrometric (MS) and tandem MS techniques, they are not able to readily identify isomeric structures. Although various separation methods provide alternatives for the analysis of glycan pools containing isomeric structures, capillary electrophoresis (CE) is often the method of choice for resolving closely related glycan structures because of its unmatched separation efficiency. It is thus natural to consider combining CE with the MS-based technologies. This review describes the utility of different CE approaches in the structural characterization of glycoproteins, and discusses the feasibility of their interface to mass spectrometry (C) 2008 Wiley Periodicals, Inc,, Mass Spec Rev 28:207-222, 2009
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