Abstract
Glycoproteins were isolated from a rat brain synaptic junction fraction by affinity chromatography on Concanavalin A-agarose. The isolated glycoproteins were digested with pronase and radiolabeled with 125I-Bolton Hunter reagent, and 125I-Concanavalin A-binding glycopeptides were isolated by chromatography on Concanavalin A-agarose. Treatment of the 125I-Concanavalin A-binding glycopeptides with either alpha-mannosidase or endo-beta-N-acetylglucosaminidase-C11 abolished their interaction with Concanavalin A. The pronase digest was reacted with endo-beta-N-acetylglucosaminidase-C11 and released oligosaccharides were reduced with NaB3H4. Following affinity chromatography on Concanavalin A-agarose, Concanavalin A-binding [3H]oligosaccharides were chromatographed on Biogel P4. Two major oligosaccharides corresponding to standard carbohydrates containing eight and five mannose residues were identified. Treatment of these oligosaccharides with alpha-mannosidase converted them to smaller saccharides having a mobility on Biogel P4 columns equal to the standard disaccharide mannose-beta-1-4-N'-acetylglucosamine. These results demonstrate that the Concanavalin A receptor activity associated with CNS synaptic junctions resides in asparagine-linked oligosaccharides of the high-mannose type.
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