Open AccessTyping of core and backbone domains of mucin‐type oligosaccharides from human ovarian‐cyst glycoproteins by 500‐MHz 1 H‐NMR spectroscopy
Author(s) -
MUTSAERS Johanna H. G. M.,
HALBEEK Herman,
VLIEGENTHART Johannes F. G.,
WU Albert M.,
KABAT Elvin A.
Publication year - 1986
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1986.tb09649.x
Subject(s) - glycoprotein , mucin , oligosaccharide , chemistry , nuclear magnetic resonance spectroscopy , carbohydrate conformation , biochemistry , typing , stereochemistry , biology , genetics
Human blood‐group A active glycoproteins from ovarian‐cyst fluid were subjected to Smith degradation and subsequent β‐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 1 H‐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 GlcNAcβ(1–3)GalNAc‐ol is described for the first time as occurring in ovarian‐cyst glycoprotein.