• Structural basis for the affinity of four insolubilized lectins, with a specificity for α-D-mannose, towards various glycopeptides with the N-glycosylamine linkage and related oligosaccharides

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    • Keywords


      Affinity chromatography; specificity of lectins; fractionation of glycopeptides

    • Abstract


      Precisions are given on the fine specificity and on the usefulness of immobilized concanavalin A,Lens culinaris, Vicia faba andPisum sativum agglutinins for fractionation of glycopeptides with the N-glycosylamine linkage.

      While insolubilized concanavalin A represents a very useful tool for the fractionation of both N-acetyllactosaminic and oligomannosidic type glycopeptides or related oligo-saccharides, immobilizedLens culinaris, as well asVicia faba orPisum sativum agglutinins allow the subfractionation of some N-acetyllactosaminic glycopeptide populations on the basis of the presence of an α-L-fucose residue substituting in C-6 position the N-acetylglucosamine residue involved in the N-glycosylamine bond.

    • Author Affiliations


      H Debray1 2 J Montreuil1 2

      1. Laboratoire de Chimie Biologique, Universite des Sciences et Techniques de Lille I et Laboratoire Associé du C.N.R.S. n† 217 - 59655, France
      2. Villeneuve d’Ascq Codex and Institut de Recherches sur le Cancer de Lille, U. 124 INSERM, BP 311, Lille Codex - 59020, France
    • Dates

  • Journal of Biosciences | News

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