Formation of homogeneous cross-linked lattices between oligomannose type glycopeptides and concanavalin A

M. Islam Khan, Lokesh Bhattacharyya, C. Fred Brewer

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

Certain oligomannose type glycopeptides have previously been shown to be bivalent for binding to concanavalin A, and to give quantitative precipitation profiles with the protein that consist of single peaks which correspond to the binding stoichiometry of glycopeptide to protein monomer (1:2) (Bhattacharyya, L., Ceccarini, C., Lorenzoni, P., and Brewer, C.F. (1987) J. Biol. Chem. 262, 1288-1293). In the present study, equimolar mixtures of two oligomannose type glycopeptides, a Man-6 and a Man-9 glycopeptide, gives a quantitative precipitation profile which shows two protein peaks. Each glycopeptide was radiolabelled with 3H or 14C, and the the precipitation profiles of the individual glycopeptides in the mixture determined. The results show that the radioactivity profile of the Man-6 glycopeptide corresponds to the first protein peak, while the radioactivity profile of the Man-9 glycopeptide corresponds to the second protein peak. The results indicate that each glycopeptide forms a unique homogeneous cross-linked lattice with the lectin which excludes the lattice of the other glycopeptide.

Original languageEnglish (US)
Pages (from-to)1076-1082
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume152
Issue number3
DOIs
StatePublished - May 16 1988

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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