MS and NMR analysis of the cross-reacting determinant glycan from Trypanosoma brucei brucei MITat 1.6 variant specific glycoprotein |
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| Authors: | B Schmitz R A Klein I A Duncan H Egge J Gunawan J Peter-Katalinic U Dabrowski J Dabrowski |
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| Affiliation: | 1. Unité de Trafic Membranaire et Pathogénèse, Institut Pasteur, Paris, France;2. Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany;1. Institute for Glyco-core Research (iGCORE), Gifu University, Gifu 501-1193, Japan;2. Institute for Integrated Cell-Material Sciences (WPI-iCeMS), Kyoto University, Kyoto 606-8507, Japan;3. Membrane Cooperativity Unit, Okinawa Institute of Science and Technology Graduate University (OIST), Onna-son, Okinawa 904-0495, Japan |
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| Abstract: | The cross-reacting determinant glycan from Trypanosoma brucei brucei MITat 1.6 is known to contain galactose, mannose and non-acetylated glucosamine. The structural elucidation of this oligosaccharide has been impeded by an unusual non-glycosidic linkage to the peptide chain and a glycosidic linkage to inositol phosphate on either side of the oligosaccharide. Using two different approaches for the isolation of the glycan, namely hydrolysis to give the oligosaccharide directly or pronase digestion to yield the glycan-containing C-terminal glycophosphopeptide, the structure of this glycan was elucidated by mass spectrometry and 1H-NMR spectroscopy. There was evidence of heterogeneity in the glycan residue. |
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