NMR studies of mannitol-terminating oligosaccharides derived by reductive alkaline hydrolysis from brain glycoproteins.
Interest in the characterisation of O-mannosyl glycan structures has been stimulated following the identification of mannitol-terminating oligosaccharides among the chains released from mammalian proteins in nervous and muscle tissues, and by the discovery of a putative human O-mannosyl transferase. Several mass spectrometry methods have been applied to structure elucidation particularly when low amounts of oligosaccharide are available for analysis. However, when sufficient amounts are available, a combination of through-bond homo- and heteronuclear, and of through-space homonuclear NMR experiments permit the complete identification of these oligosaccharide sequences. We describe here the assignment of 1H and 13C NMR chemical shifts from such experiments for four mannitol-terminating oligosaccharide alditols, GlcNAcbeta-(1-->2)Manol, Galbeta-(1-->4)GlcNAcbeta-(1-->2)Manol, Galbeta-(1-->4)[Fucalpha-(1-->3)]GlcNAcbeta-(1-->2)Manol and NeuAcalpha-(2-->3)Galbeta-(1-->4)GlcNAcbeta-(1-->2)Manol, that were released from brain glycopeptides by alkaline borohydride treatment.
Kogelberg
H
H
The Glycosciences Laboratory, Imperial College School of Medicine, Northwick Park Hospital, Harrovw, Middlesex, UK. h.kogelberg@ic.ac.uk
Chai
W
W
Feizi
T
T
Lawson
A M
AM
D000818:Animals; D001923:Brain Chemistry; D002240:Carbohydrate Sequence; D006020:Glycopeptides / Q000737:chemistry; D006023:Glycoproteins / Q000737:chemistry*; D008353:Mannitol / Q000031:analogs & derivatives*; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D009844:Oligosaccharides / Q000737:chemistry*; D011817:Rabbits; D013402:Sugar Alcohols / Q000737:chemistry
D006020:Glycopeptides; D006023:Glycoproteins; D009419:Nerve Tissue Proteins; D009844:Oligosaccharides; D013402:Sugar Alcohols; D008353:Mannitol