Purification and characterization of carbohydrate-binding peptides from Lotus tetragonolobus and Ulex europeus seed lectins using affinity chromatography.
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.
Konami
Y
Y
Division of Chemical Toxicology and Immunochemistry, Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Yamamoto
K
K
Osawa
T
T
D000595:Amino Acid Sequence; D002241:Carbohydrates / Q000737:chemistry / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D007887:Fabaceae / Q000737:chemistry*; D037102:Lectins / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification*; D037121:Plant Lectins; D010946:Plants, Medicinal; D012639:Seeds / Q000737:chemistry*
D002241:Carbohydrates; D037102:Lectins; D010455:Peptides; D037121:Plant Lectins