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Journal Article

MS and NMR analysis of the cross-reacting determinant glycan from Trypanosoma brucei brucei MITat 1.6 variant specific glycoprotein

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Dabrowski,  Ursula
Department of Organic Chemistry, Max Planck Institute for Medical Research, Max Planck Society;

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Dabrowski,  Janusz
Department of Organic Chemistry, Max Planck Institute for Medical Research, Max Planck Society;

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https://www.sciencedirect.com/science/article/pii/0006291X87907546/pdf?md5=93385e8ca9e11de32d4ce9485aa631ac&pid=1-s2.0-0006291X87907546-main.pdf
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https://doi.org/10.1016/0006-291X(87)90754-6
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Citation

Schmitz, B., Klein, R. A., Duncan, I. A., Egge, H., Gunawan, J., Peter-Katalinic, J., et al. (1987). MS and NMR analysis of the cross-reacting determinant glycan from Trypanosoma brucei brucei MITat 1.6 variant specific glycoprotein. Biochemical and Biophysical Research Communications, 146(3), 1055-1063. doi:10.1016/0006-291X(87)90754-6.


Cite as: https://hdl.handle.net/21.11116/0000-0007-9950-2
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.