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Tandem Mass Spectrometry of N-linked Glycans from Human Immunoglobulin G  

Joo, Hwang-Soo (School of Chemical & Biological Engineering, Seoul National University)
Kim, Yun-Gon (Interdisciplinary Program for Biochemical Engineering and Biotechnology, Seoul National University)
Jang, Kyoung-Soon (Interdisciplinary Program for Biochemical Engineering and Biotechnology, Seoul National University)
Kim, Byung-Gee (School of Chemical & Biological Engineering, Seoul National University)
Publication Information
KSBB Journal / v.22, no.4, 2007 , pp. 234-238 More about this Journal
Abstract
We used electrospary ionization ion trap tandem mass spectrometry (ESI-IT tandem MS) to structural elucidation of three different biantennary-type glycans having zero, one, two galactoses (G0, G1, G2). The highest fragment ion in the MS/MS spectra of three glycans was produced by 0,2-ring cleavage of fucose-linked N-acetylglucosamine (GlcNAc) in reducing end. The fragment ions both from precursor ions and 0,2-ring cleaved ions ($^{0.2}An$; n=5 for G0, n=6 for G1 and G2) were not overlapped each other. As results of $MS^n$ analyses, tandem fragmentation trees of each glycans were generated and 2,4-ring cleavages ($^{2.4}A_6$) were occurred in GlcNAc linked to reducing end GlcNAc. This structural elucidation and fragmentation study of N-linked glycans by tandem mass spectrometry can be applied to structural analysis of more complicated glycans.
Keywords
Tandem mass spectrometry; human immunoglobulin G; N-linked glycan;
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