Abstract

Young Researchers' Sessions

Day 3, May 17（Wed.）　09:15-09:30　Room C (Room 1009)

3C-O-0915（2P-14）　　PDF

O-glycan analysis of intact glycoprotein by MALDI-ISD MS

(Hokkaido Univ.)
^oShogo Urakami, Hiroshi Hinou

Protein glycosylation are classified into N-glycans and O-glycans based on the differences in the amino acids and are involved in various biological processes such as infection and disease. These specific changes in glycans have been used as predictive and diagnostic markers of diseases. Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) enables high-sensitivity and high-resolution analysis and has been widely used for glycan analysis of glycoproteins. However, glycan analysis requires complicated pretreatment processes such as digestion and purification, thus making the measurement time-consuming. In our previous study, we succeeded in measuring glycans of intact N-linked glycoproteins by MALDI-In Source Decay (ISD) MS. This technique enables glycan fragmentation and glycan selective ionization using specific matrices. However, MALDI-ISD MS requires high laser irradiation power and tends to produce noise in the low-molecular-weight region below m/z 1000, making it difficult to measure short O-glycans. In this study, we succeeded in exploring the matrix for selective glycan detection by MALDI-ISD MS, even in the low-molecular-weight region. By this investigation, we demonstrated a rapid and simple method for O-glycan analysis from intact O-linked glycopeptide and glycoprotein without any pretreatment. MS/MS analysis also enabled the identification of the constituent monosaccharide residues of O-glycan signals from intact glycoprotein.