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Current Proteomics

Editor-in-Chief

ISSN (Print): 1570-1646
ISSN (Online): 1875-6247

Analysis of Glycosaminoglycans Using Mass Spectrometry

Author(s): Gregory O. Staples and Joseph Zaia

Volume 8, Issue 4, 2011

Page: [325 - 336] Pages: 12

DOI: 10.2174/157016411798220871

Price: $65

Abstract

The glycosaminoglycans (GAGs) are linear polysaccharides expressed on animal cell surfaces and in extracellular matrices. Their biosynthesis is under complex control and confers a domain structure that is essential to their ability to bind to protein partners. Key to understanding the functions of GAGs are methods to determine accurately and rapidly patterns of sulfation, acetylation and uronic acid epimerization that correlate with protein binding or other biological activities. Mass spectrometry (MS) is particularly suitable for the analysis of GAGs for biomedical purposes. Using modern ionization techniques it is possible to accurately determine molecular weights of GAG oligosaccharides and their distributions within a mixture. Methods for direct interfacing with liquid chromatography have been developed to permit on-line mass spectrometric analysis of GAGs. New tandem mass spectrometric methods for fine structure determination of GAGs are emerging. This review summarizes MS-based approaches for analysis of GAGs, including tissue extraction and chromatographic methods compatible with LC/MS and tandem MS.

Keywords: Mass spectrometry, dermatan sulfate, glycosaminoglycan, Chondroitin sulfate, heparan sulfate, heparin, proteoglycan, hyaluronan, keratan sulfate, Fibroblast growth factor, Graphitized carbon chromatography

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