Abstract
The carbohydrate binding properties of jacalin lectin were examined using RAF9 cell-derived d-[6- 3H]glucosamine-radiolabeled total glycopeptides containing N-linked and O-linked oligosaccharides. The binding of N-linked glycopeptides to jacalin was abolished by treatment of α-galactosidase whereas O-linked glycopeptides were still bound lectin after this treatment. The removal of O-linked oligosaccharides by mild alkaline/borohydride treatment completely eliminated the lectin binding of α-galactosidase treated glycopeptides. These results demonstrate that jacalin interacts with cellular glycopeptides containing N-linked oligosaccharides with terminal α-galactose residues as well as glycopeptides containing O-linked oligosaccharides.
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