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Bovine Pituitary Membrane Glycoproteins Contain β‐ N ‐Acetylgalactosaminylated N‐Linked Sugar Chains
Author(s) -
Taka Junko,
Sato Takeshi,
Sakiyama Toru,
Fujisawa Hirosuke,
Furukawa Kiyoshi
Publication year - 1996
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1996.66020852.x
Subject(s) - glycoprotein , exoglycosidase , biochemistry , lectin , membrane glycoproteins , chemistry , agglutinin , glycan , biology
Bovine pituitary glycoprotein hormones contain unique N‐linked sugar chains with GalNAcβ1 → 4GlcNAc structure in their outer chain moieties. In the present study, whether bovine pituitary membrane glycoproteins contain the sugar chains with the disaccharide structure was investigated. Western blot analysis of the membrane glycoproteins using Wistaria floribunda agglutinin (WFA), which binds oligosaccharides terminating with β‐ N ‐acetylgalactosamine residue(s), showed that most protein bands detected with Coomassie Brilliant Blue staining bind to WFA. However, no WFA binding was observed for the bands after treatment of the blotted filter with jack bean β‐ N ‐acetylhexosaminidase or N ‐Glycanase. The WFA‐positive bands were also detected in membrane glycoprotein samples from bovine cerebrum, cerebellum, and medulla oblongata, although their expression levels were low. Structural analysis of the oligosaccharides released by hydrazinolysis from the pituitary membrane glycoproteins by serial lectin column chromatography and sequential exoglycosidase digestion revealed that the major oligosaccharides, which bound to a WFA‐agarose column, are of biantennary complex type with one and two GalNAcβ1 → 4GlcNAc groups in their outer chain moieties. These results indicate that the β‐ N ‐acetylgalactosaminylation is not unique to the glycoprotein hormones but occurs to most bovine pituitary glycoproteins.