Related Experiment Video
Updated: Jun 26, 2026

Mass Spectrometric Analysis of Glycosphingolipid Antigens
Published on: April 16, 2013
Use of FTIR and mass spectrometry for characterization of glycated caseins
Christine M Oliver1, Ashwini Kher, Don McNaughton
1School of Chemistry, Monash University, Clayton, VIC 3800, Australia. Christine1.Olivier@csiro.au
Abstract:
This study investigates the potential of Fourier transform infrared spectroscopy (FTIR) to monitor glycation-induced changes in protein structure. Aqueous solutions of sodium caseinate and glucose (1:2 w/w, pH 6.7) were heated at 90 degrees C for 0, 10, 20, 40 and 60 min. Evidence for caseinate glycation was obtained by mass spectrometry techniques (electrospray (ESI) and matrix-assisted laser desorption ionisation (MALDI)). FTIR was able to discriminate between glycated and non-glycated sodium caseinate, when the data were analysed by multivariate statistical methods; principal component analysis (PCA) and soft independent modelling of class analogy (SIMCA). The techniques used were complementary and provided different levels of information about the glycated samples.
Related Concept Videos
MALDI-TOF Mass Spectrometry
Mass Spectrometry: Complex Analysis
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
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...