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  • Title: Interactions of concanavalin A with a trimannosyl oligosaccharide fragment of complex and high mannose type glycopeptides.
    Author: Brewer F, Bhattacharyya L, Brown RD, Koenig SH.
    Journal: Biochem Biophys Res Commun; 1985 Mar 29; 127(3):1066-71. PubMed ID: 3838666.
    Abstract:
    It has previously been reported that the binding interactions of concanavalin A with a purified high mannose type glycopeptide from ovalbumin differs from that with simple mono- and oligosaccharides (Brewer, C.F. (1979) Biochem. Biophys. Res. Commun. 90, 117-122). We now report studies with a synthetic analog of complex type glycopeptides, and a synthetic trimannosyl oligosaccharide fragment that is common to both complex and high mannose type glycopeptides. We find that both synthetic oligosacchardes undergo similar interactions with concanavalin A which mimic the effects of binding corresponding larger glycopeptides. Furthermore, the relative affinity of the trimannosyl oligosaccharide is 130-fold greater than the binding of methyl-alpha-D-mannopyranoside. The results indicate that the trimannosyl oligosaccharide is a unique structural element recognized by the lectin.
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