Precipitation of Concanavalin A by a high mannose type glycopeptide

Lokesh Bhattacharyya, Curtis F. Brewer

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

The interactions of a high mannose type glycopeptide with Concanavalin A has been investigated by quantitative precipitation analysis. The equivalence points of the precipitin curves indicate that the glycopeptide is bivalent for lectin binding. These results and others demonstrate that there are two lectin binding sites per molecule of the glycopeptide: one site on the α(1-6) arm of the core β-mannose residue involving a trimannosyl moiety, and another site on the α(1-3) arm of the core β-mannose residue involving an α(1-2) mannobiosyl group. The two sites are unequal in their affinities, and bind by different mechanisms. These results are related to the possible structure-function properties of high mannose type of glycopeptides on the surface of cells.

Original languageEnglish (US)
Pages (from-to)670-674
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume137
Issue number2
DOIs
StatePublished - Jun 13 1986

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Glycopeptides
Mannose
Concanavalin A
Lectins
Precipitins
Binding Sites
Molecules

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Precipitation of Concanavalin A by a high mannose type glycopeptide. / Bhattacharyya, Lokesh; Brewer, Curtis F.

In: Biochemical and Biophysical Research Communications, Vol. 137, No. 2, 13.06.1986, p. 670-674.

Research output: Contribution to journalArticle

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