MALDI mass spectrometry as a tool for characterizing glycosaminoglycan oligosaccharides and their interaction with proteins.
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.
Sturiale
L
L
Istituto di Chimica e Biochimica, G. Ronzoni Research Institute, Milan, Italy.
Naggi
A
A
Torri
G
G
D000818:Animals; D005346:Fibroblast Growth Factors / Q000737:chemistry / Q000378:metabolism; D006025:Glycosaminoglycans / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
D006025:Glycosaminoglycans; D009844:Oligosaccharides; D010455:Peptides; D005346:Fibroblast Growth Factors