Current Proteomics

Bernd Rehm  
Institute of Molecular BioSciences Massey University
Private Bag 11222
Palmerston North
New Zealand


Analysis of Glycosaminoglycans Using Mass Spectrometry

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


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

Order Reprints Order Eprints Rights & PermissionsPrintExport

Article Details

Year: 2011
Page: [325 - 336]
Pages: 12
DOI: 10.2174/157016411798220871
Price: $58