The primary structure of the Cytisus scoparius seed lectin and a carbohydrate-binding peptide.
The complete amino acid sequence of 2-acetamido-2-deoxy-D-galactose-binding Cytisus scoparius seed lectin II (CSII) was determined using a protein sequencer. After digestion of CSII with endoproteinase Lys-C or Asp-N, the resulting peptides were purified by reversed-phase high performance liquid chromatography (HPLC) and then subjected to sequence analysis. Comparison of the complete amino acid sequence of CSII with the sequences of other leguminous seed lectins revealed regions of extensive homology. The amino acid residues of concanavalin A (Con A) involved in the metal binding site are highly conserved among those of CSII. A carbohydrate-binding peptide of CSII was obtained from the endoproteinase Asp-N digest of CSII by affinity chromatography on a column of GalNAc-Gel. This peptide was retained on the GalNAc-Gel column and was presumed to have affinity for the column. The amino acid sequence of the retarded peptide was determined using a protein sequencer. The retarded peptide was found to correspond to the putative metal-binding region of Con A. These results strongly suggest that this peptide represents the carbohydrate-binding and metal ion-binding sites of CSII.
Konami
Y
Y
Division of Chemical Toxicology and Immunochemistry, Faculty of Pharmaceutical Sciences, University of Tokyo.
Yamamoto
K
K
Osawa
T
T
Irimura
T
T
D000595:Amino Acid Sequence; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry*; D002846:Chromatography, Affinity; D007887:Fabaceae; D006031:Glycosylation; D037102:Lectins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D037121:Plant Lectins; D010946:Plants, Medicinal; D011956:Receptors, Cell Surface; D017386:Sequence Homology, Amino Acid
D002352:Carrier Proteins; D037102:Lectins; D010455:Peptides; D037121:Plant Lectins; D011956:Receptors, Cell Surface; C055213:saccharide-binding proteins