Tandem Mass Spectrometry of N-linked Glycans from Human Immunoglobulin G
2007
Joo, H.S. (Seoul National University, Seoul, Republic of Korea) | Kim, Y.G. (Seoul National University, Seoul, Republic of Korea) | Jang, K.S. (Seoul National University, Seoul, Republic of Korea) | Kim, B.G. (Seoul National University, Seoul, Republic of Korea), E-mail: [email protected]
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 (∨0.2An; 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 (∨2,4A∧6) were occurred in GlcNAc linked to reducing end GlcNAc.
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