Purification and properties of a novel fucose-specific hemagglutinin of Aleuria aurantia.
A fucose-binding lectin from fruiting bodies of Aleuria aurantia was purified by affinity chromatography by using the H-active glycopeptide of desialyzed porcine submaxillary mucine coupled to Sepharose 4B and eluting with L-fucose. Homogeneity of the active protein was confirmed by polyacrylamide gel electrophoresis, isoelectric focusing, column chromatography using Sephadex G-100, and ultracentrifugal analyses. It has a molecular weight of 72 000 and is proposed to be a dimer of identical subunits, each of which has combining site of uniform affinity. Chemical analyses revealed the absence of the sulfur-containing amino acid and carbohydrate, neutral and amino sugar, in the lectin molecule. It agglutinated human erythrocytes of all ABO and Lewis types, Bombay phenotype, and group O cells treated with alpha (1 leads to 2)-fucosidase. In double-diffusion experiments, the lectin formed a single precipitin line which fused with all of the fucose-containing blood-group substances tested, including the alpha-fucosidase-treated materials. These findings together with the results of hemagglutination and precipitation studies indicate that the lectin combines the terminal fucose in the carbohydrate chain but doses not require a particular linkage to the penultimate sugar moiety.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001789:Blood Group Antigens / Q000276:immunology; D005643:Fucose; D006385:Hemagglutination Inhibition Tests; D006386:Hemagglutination Tests; D037102:Lectins / Q000302:isolation & purification; D008970:Molecular Weight; D009077:Mucins; D009844:Oligosaccharides; D037121:Plant Lectins; D010944:Plants / Q000032:analysis*; D013552:Swine
D000596:Amino Acids; D001789:Blood Group Antigens; D037102:Lectins; D009077:Mucins; D009844:Oligosaccharides; D037121:Plant Lectins; D005643:Fucose