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KMID : 0380020070220040234
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Korean Journal of Biotechnology and Bioengineering
2007 Volume.22 No. 4 p.234 ~ p.238
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Tandem Mass Spectrometry of N-linked Glycans from Human Immunoglobulin G
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Kim Byung-Gee
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Abstract
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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 (; n=5 for G0, n=6 for G1 and G2) were not overlapped each other. As results of analyses, tandem fragmentation trees of each glycans were generated and 2,4-ring cleavages () 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
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KEYWORD
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Tandem mass spectrometry, human immunoglobulin G, N-linked glycan
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