Literature DB >> 1618731

Carbohydrate-binding peptides from several anti-H(O) lectins.

K Yamamoto1, Y Konami, T Osawa, T Irimura.   

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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Year:  1992        PMID: 1618731     DOI: 10.1093/oxfordjournals.jbchem.a123775

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  2 in total

1.  A putative carbohydrate-binding domain of the lactose-binding Cytisus sessilifolius anti-H(O) lectin has a similar amino acid sequence to that of the L-fucose-binding Ulex europaeus anti-H(O) lectin.

Authors:  Y Konami; K Yamamoto; T Osawa; T Irimura
Journal:  Glycoconj J       Date:  1995-04       Impact factor: 2.916

2.  Mammalian Cell Surface Display as a Novel Method for Developing Engineered Lectins with Novel Characteristics.

Authors:  Keisuke Soga; Hirohito Abo; Sheng-Ying Qin; Takuya Kyoutou; Keiko Hiemori; Hiroaki Tateno; Naoki Matsumoto; Jun Hirabayashi; Kazuo Yamamoto
Journal:  Biomolecules       Date:  2015-07-20
  2 in total

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