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  • Title: Carbohydrate-binding peptides from several anti-H(O) lectins.
    Author: Yamamoto K, Konami Y, Osawa T, Irimura T.
    Journal: J Biochem; 1992 Apr; 111(4):436-9. PubMed ID: 1618731.
    Abstract:
    Peptide fragments have been obtained from L-fucose-binding anti-H(O) lectins [Lotus tetragonolobus lectin (LTA) and Ulex europeus lectin I (UEA-I)] and di-N-acetylchitobiose-binding anti-H(O) lectins [Ulex europeus lectin II (UEA-II) and Laburnum alpinum lectin I (LAA-I)] by treatment with endoproteinase Asp-N or Lys-C. The peptide fragments were fractionated by affinity chromatography on a column of Fuc-Gel for LTA and UEA-I, and on a column of N-acetyl-D-glucosamine oligomer-Sepharose for UEA-II and LAA-I. The peptides with affinity for these columns were identified by peptide sequencing. All of these retarded peptides were found to be parts of the metal-binding regions of these lectins. It is strongly suggested that these peptides represent the carbohydrate-binding and metal ion-binding sites of legume lectins, respectively.
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