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- W1986200044 abstract "The structural requirements for the binding of oligosaccharides and glycopeptides to immobilized Vicia faba agglutinin were investigated, and its carbohydrate specificity was compared with the specificities of the α-d-mannose-binding lectins concanavalin A, Lens culinaris agglutinin, and Pisum sativum agglutinin. Immobilized Vicia faba agglutinin can interact only with biantennary glycopeptides possessing an α-l-fucosyl group attached to the l-asparagine-linked 2-acetamido-2-deoxy-β-d-glucopyranosyl residue. An l-asparagine residue is essential for high affinity-binding to Vicia faba agglutinin-Sepharose. In addition, the enzymic exposure of a (nonreducing) terminal α-d-mannosyl group enhances the interaction of the glycopeptide with immobilized Vicia faba agglutinin. This sugar-binding specificity of immobilized Vicia faba agglutinin is similar to that of immobilized Pisum sativum agglutinin." @default.
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- W1986200044 date "1984-07-01" @default.
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- W1986200044 title "Structural requirements for the binding of glycopeptides to immobilized Vicia faba (fava) lectin" @default.
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- W1986200044 doi "https://doi.org/10.1016/0008-6215(84)85316-1" @default.
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