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Semin Thromb Hemost 2001; 27(5): 465-472
DOI: 10.1055/s-2001-17957
Copyright © 2001 by Thieme Medical Publishers, Inc., 333 Seventh Avenue, New York, NY 10001, USA. Tel.: +1(212) 584-4662

MALDI Mass Spectrometry as a Tool for Characterizing Glycosaminoglycan Oligosaccharides and their Interaction with Proteins

Luisa Sturiale, Annamaria Naggi, Giangiacomo Torri
  • Istituto di Chimica e Biochimica, G. Ronzoni Research Institute, Milan, Italy
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Publication History

Publication Date:
22 October 2001 (online)

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ABSTRACT

Matrix-Assisted Laser Desorption Ionization (MALDI) mass spectrometry (MS) has emerged as a powerful, sensitive technique for structural analysis of glycosaminoglycans (GAGs) and their fractions and fragments. Whereas the molecular size of low sulfated or nonsulfated species (such as low-molecular weight [LMW] K5 polysaccharides) can be directly determined up to molecular weights (MWs) of 12 kD, polysulfated species require complexing with a basic polypeptide and at present can be characterized (in terms of both MW and end residues) up to the size of a decasaccharide, even in complex mixtures. MALDI spectra of GAG oligosaccharides in the presence of a complexing protein permit to assess binding to the protein and the presence of multimeric complexes.

KEYWORD

Glycosaminoglycans - MALDI mass spectrometry - molecular weight distributions - protein-binding oligosaccharides

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