Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
Human blood-group A active glycoproteins from ovarian-cyst fluid were subjected to Smith degradation and subsequent beta-elimination. The resulting oligosaccharide-alditols represent the core and backbone domains of the O-linked carbohydrate chains. Nine of these, ranging in size from disaccharides to hexasaccharides, were investigated by 1H-NMR spectroscopy. Their primary structures could be adequately characterized. In particular, the core types, i.e. the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences, were unambiguously identified. The core type GlcNAc beta(1-3)GalNAc-ol is described for the first time as occurring in ovarian-cyst glycoprotein.
J H
JH
Mutsaers
H
H
van Halbeek
J F
JF
Vliegenthart
A M
AM
Wu
E A
EA
Kabat
D000017:ABO Blood-Group System; D002240:Carbohydrate Sequence; D005260:Female; D006023:Glycoproteins / Q000032:analysis*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D009077:Mucins / Q000032:analysis*; D009844:Oligosaccharides / Q000032:analysis*; D010048:Ovarian Cysts / Q000032:analysis*
D000017:ABO Blood-Group System; D006023:Glycoproteins; D009077:Mucins; D009844:Oligosaccharides