Purification and characterization of a mitogenic lectin and a lectin-binding protein from Vicia sativa.
From the seeds of Vicia sativa, a novel mitogenic lectin was isolated. Purification was carried out by affinity chromatography on Sephadex G-100. The tetrameric lectin is a glycoprotein with a molecular weight of Mr 40 000; it consists of two large beta-subunits (Mr 14 000) and two small alpha-subunits (Mr 6000). The N-terminal sequence of both subunits and their amino acid compositions were determined. The lectin agglutinates human erythrocytes, preferring group B, and erythrocytes from rabbits and horses; no agglutination takes place with sheep erythrocytes. Agglutination is inhibited by mono-, di- and tri-saccharides with the configuration of glucose at the free 4-hydroxyl group. The lectin stimulates mitosis in lymphocytes of mice. From the seeds of the same plant, a protein was isolated which binds to the lectin described above. The lectin binder consists of subunits with a molecular weight of 53 500.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates; D006023:Glycoproteins / Q000302:isolation & purification; D006386:Hemagglutination Tests; D006736:Horses; D006801:Humans; D037102:Lectins / Q000302:isolation & purification*; D008213:Lymphocyte Activation; D046911:Macromolecular Substances; D051379:Mice; D008934:Mitogens; D008970:Molecular Weight; D037121:Plant Lectins; D011817:Rabbits; D012639:Seeds / Q000032:analysis; D012756:Sheep; D013045:Species Specificity
D000596:Amino Acids; D002241:Carbohydrates; D006023:Glycoproteins; D037102:Lectins; D046911:Macromolecular Substances; D008934:Mitogens; D037121:Plant Lectins