title: Studies on lectins. LII. Isolation and characterization of the lectin from rye germ (Secale cereale L.).
abstract: Rye germ lectin was isolated by extraction of defatted rye germ, fractionation of the extract by ammonium sulfate precipitation, affinity chromatography of the active substances on chitin-beta-glucan and gel filtration on Sephadex G-50. The lectin shows erythroagglutinating activity at a minimum concentration of 2.5 micrograms/ml. The erythroagglutinating activity is the same against human red blood cells of all types of the ABO system and is inhibited by N-acetyl-D-glucosamine. The lectin has no mitogenic activity against mouse splenic lymphocytes. According to the results of polyacrylamide gel electrophoresis the lectin obtained is a mixture of three very similar isolectins of equal erythroagglutinating activity. Sedimentation analysis indicates homogeneity of the lectin preparation; the molecular weight was 56000 as estimated by sedimentation equilibrium. In the presence of urea and sodium dodecyl sulfate the lectin dissociates into 2 types of subunits with molecular weights of 35000 and 19000. The rye germ lectin contains about 2% of neutral sugar and 1% of D-glucosamine. The amino acid composition of the lectin is characterized by a very high content of glycine and half cystine and a low content of apolar amino acids. N-terminal amino acids of the lectin are apparently blocked.
mesh_terms: D000117:Acetylglucosamine / Q000494:pharmacology; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002523:Edible Grain / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D006385:Hemagglutination Inhibition Tests; D006388:Hemagglutinins; D006801:Humans; D037102:Lectins / Q000032:analysis / Q000302:isolation & purification* / Q000494:pharmacology; D037121:Plant Lectins; D012434:Secale / Q000032:analysis*
chemical_list: D006388:Hemagglutinins; D037102:Lectins; D037121:Plant Lectins; D000117:Acetylglucosamine