Related Experiment Video
Updated: Sep 22, 2026

Mass Spectrometric Analysis of Glycosphingolipid Antigens
Published on: April 16, 2013
MALDI mass spectrometry as a tool for characterizing glycosaminoglycan oligosaccharides and their interaction with
1Istituto di Chimica e Biochimica, G. Ronzoni Research Institute, Milan, Italy.
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.
Related Concept Videos
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
MALDI-TOF Mass Spectrometry
Peptide Identification Using Tandem Mass Spectrometry
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
Matrix-Assisted Laser Desorption Ionization (MALDI)

