A two-dimensional 1H-n.m.r. (500 MHz) and 13C-n.m.r. (125 MHz) study of 
N-linked glycopeptides derived from calf fetuin

Berman, Elisha; Dabrowski, Ursula; Dabrowski, Janusz

doi:10.1016/0008-6215(88)84053-9

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A two-dimensional 1H-n.m.r. (500 MHz) and 13C-n.m.r. (125 MHz) study of N-linked glycopeptides derived from calf fetuin

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Berman, Elisha
Max Planck Institute for Medical Research, Max Planck Society;

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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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Citation

Berman, E., Dabrowski, U., & Dabrowski, J. (1988). A two-dimensional 1H-n.m.r. (500 MHz) and 13C-n.m.r. (125 MHz) study of N-linked glycopeptides derived from calf fetuin. Carbohydrate Research, 176(1), 1-15. doi:10.1016/0008-6215(88)84053-9.

Cite as: https://hdl.handle.net/21.11116/0000-000A-53E1-A

Abstract

The oligosaccharide part of an N-linked triantennary glycopeptide from calf fetuin with fourteen carbohydrate residues and its smaller derivatives obtained by successive enzymic cleavage of the terminal residues were investigated using 2D 1H-n.m.r. (500 MHz) and 13C-n.m.r. (125 MHz) spectroscopy. Assignments have been made of the resonances of almost all the protons of the constituent carbohydrate residues in these glycopeptides. A comparison of the 1H chemical shifts and coupling constants, as determined from the cross-peaks, has shown the dependence of these parameters on the interactions of spatially related neighbouring carbohydrates. Small conformational changes take place upon elongation of the oligosaccharide side-chains.