Interactions of concanavalin a with a trimannosyl oligosaccharide fragment of complex and high mannose type glycopeptides

Fred Brewer, Lokesh Bhattacharyya, Rodney D. Brown, Seymour H. Koenig

Research output: Contribution to journalArticle

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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 oligosaccharides fragment that is common to both complex and high mannose type glycopeptides. We find that both synthetic oligosaccharides undergo similar interactions with concanavalin A which mimic the effects of binding corresponding larger glycopeptides. Furthermore, the relative affinity of the trimannosyl oligosaccharides is 130-fold greater than the binding of methyl-α-D-mannopyranoside. The results indicate that the trimannosyl oligosaccharide is a unique structural element recognized by the lectin.

Original languageEnglish (US)
Pages (from-to)1066-1071
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Mar 29 1985


ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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