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MALDI mass spectrometry as a tool for characterizing glycosaminoglycan oligosaccharides and their interaction with proteins (Articolo in rivista)
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- MALDI mass spectrometry as a tool for characterizing glycosaminoglycan oligosaccharides and their interaction with proteins (Articolo in rivista) (literal)
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- 2001-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1055/s-2001-17957 (literal)
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L.Sturiale, A.Naggi, G.Torri (2001)
MALDI mass spectrometry as a tool for characterizing glycosaminoglycan oligosaccharides and their interaction with proteins
in Seminars in thrombosis and hemostasis (Print); Thieme Medical Publisher, New York (Stati Uniti d'America)
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- L.Sturiale, A.Naggi, G.Torri (literal)
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- Istituto di Chimica e Biochimica, G. Ronzoni Research Institute, Milan, Italy (literal)
- Titolo
- MALDI mass spectrometry as a tool for characterizing glycosaminoglycan oligosaccharides and their interaction with proteins (literal)
- 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. (literal)
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