title: Carbohydrate-binding peptides from several anti-H(O) lectins.
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.
authors.affiliation: Division of Chemical Toxicology and Immunochemistry, Faculty of Pharmaceutical Sciences, University of Tokyo.
authors.forename: K
authors.initials: K
authors.lastname: Yamamoto
authors.forename: Y
authors.initials: Y
authors.lastname: Konami
authors.forename: T
authors.initials: T
authors.lastname: Osawa
authors.forename: T
authors.initials: T
authors.lastname: Irimura
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002846:Chromatography, Affinity; D003208:Concanavalin A / Q000737:chemistry / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D037121:Plant Lectins; D012689:Sequence Homology, Nucleic Acid
chemical_list: C039340:Bauhinia purpurea lectin; D037102:Lectins; D010446:Peptide Fragments; D037121:Plant Lectins; C036850:Ulex europaeus lectins; C027112:fucose-binding lectin; D003208:Concanavalin A; C070194:lectin I, Laburnum alpinum; D010450:Endopeptidases