Isolation and properties of a lectin from sainfoin (Onobrychis viciifolia, Scop.).
A glycoprotein capable of binding simple carbohydrates and causing hemagglutination has been isolated from seeds of the legume plant sainfoin (Onobrychis viciifolia, Scop. var Eski). The phytolectin was prepared by affinity chromatography of pH 7.0 sodium phosphate extracts on columns of Sepharose-4B containing covalently attached D-mannose. Molecular weight determinations showed the lectin to be a dimer consisting of 26 000 dalton, non-covalently associated monomers. Amino acid analyses indicated high amounts of aspartate, glutamate, threonine and serine which accounted for 41% of all amino acids. One residue of cysteine was present and methionine was totally absent. The lectin contained 2.6% (w/w) neutral carbohydrate and two residues of N-acetylglucosamine/monomer. Carbohydrate-binding specificity was directed toward D-mannose and D-glucose and their alpha-glycosidic derivatives. The purified protein agglutinated cat erythrocytes at 5 micrograms/ml. Antiserum to seed lectin showed a single common immunoprecipitation line in Ouchterlony double diffusion against both the seed and root antigen. Lectin isolated from sainfoin seedling roots showed molecular weight, amino acid and carbohydrate values similar to that of the seed lectin.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D002415:Cats; D055598:Chemical Phenomena; D002621:Chemistry; D004912:Erythrocytes / Q000187:drug effects; D007887:Fabaceae / Q000032:analysis*; D037102:Lectins / Q000302:isolation & purification* / Q000494:pharmacology; D008970:Molecular Weight; D037121:Plant Lectins; D010940:Plant Proteins / Q000032:analysis; D010946:Plants, Medicinal; D012639:Seeds / Q000032:analysis
D000596:Amino Acids; D002241:Carbohydrates; D037102:Lectins; D037121:Plant Lectins; D010940:Plant Proteins