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Updated: Jan 11, 2026

Mass Spectrometric Analysis of Glycosphingolipid Antigens
Published on: April 16, 2013
MALDI mass spectrometry analysis of N-glycans through DMTMM-mediated benzylamidation and Girard's reagent P labeling
Minju Kim1, Eun Ju Lee1, Sohee Yoon2
1Department of Chemical Engineering and Applied Chemistry, Chungnam National University, Daejeon 34134, South Korea. haemin.park@cnu.ac.kr.
Abstract:
Glycosylation is one of the major post-translational modifications of proteins and plays important roles in diverse biological processes, including cell signaling and recognition. Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) has been widely used to analyze glycans formed through glycosylation because it generates mainly singly charged ions and offers relatively high ionization efficiency for glycans. In this study, we present a method for MALDI-MS-based N-glycan analysis with 4-(4,6-dimethoxy-1,3,5-triazin-2-yl)-4-methylmorpholinium chloride (DMTMM)-mediated stabilization of sialic acids and permanent cationic labeling of the glycan reducing ends. This method allows the sensitive measurement of intact N-glycans released from glycoproteins and may contribute to the characterization of biotherapeutic glycosylation in the pharmaceutical industry.
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