Purification and characterization of carbohydrate-binding peptides from Lotus tetragonolobus and Ulex europeus seed lectins using affinity chromatography

J Chromatogr. 1992 Apr 24;597(1-2):213-9. doi: 10.1016/0021-9673(92)80113-9.

Abstract

Carbohydrate-binding peptides of several anti-H(O) leguminous lectins were obtained from endoproteinase Asp-N or Lys-C digests of L-fucose-binding Lotus tetragonolobus lectin (LTA) and Ulex europeus lectin I (UEA-I) and from that of a di-N-acetylchitobiose-binding Ulex europeus lectin II (UEA-II) by affinity chromatography on columns of Fuc-Gel (for LTA and UEA-I) and on a column of a mixture of several oligomers of N-acetyl-D-glucosamine (GlcNAc) coupled to Sepharose 4B (GlcNAc oligomer-Sepharose 4B) (for UEA-II). These peptides were retained on the Fuc-Gel or GlcNAc oligomer-Sepharose 4B column and were presumed to have an affinity for the columns. The amino acid sequences of the retarded peptides were determined using a protein sequencer.

MeSH terms

  • Amino Acid Sequence
  • Carbohydrates / chemistry
  • Carbohydrates / isolation & purification*
  • Chromatography, Affinity
  • Fabaceae / chemistry*
  • Lectins / isolation & purification*
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / isolation & purification*
  • Plant Lectins
  • Plants, Medicinal*
  • Seeds / chemistry*

Substances

  • Carbohydrates
  • Lectins
  • Peptides
  • Plant Lectins