The
carbohydrate-binding specificity of
Aleuria aurantia lectin was investigated by analyzing the behavior of a variety of
fucose-containing
oligosaccharides on an A. aurantia
lectin-
Sepharose column. Studies with complex-type
oligosaccharides obtained from various
glycoproteins by hydrazinolysis and their partial degradation fragments indicated that the presence of the alpha-fucosyl residue linked at the C-6 position of the proximal
N-acetylglucosamine moiety is indispensable for binding to the
lectin column. Binding was not affected by the structures of the outer chain moieties nor by the presence of the bisecting
N-acetylglucosamine residue. These results indicated that A. aurantia
lectin-
Sepharose is useful for the group separation of mixtures of complex-type
asparagine-linked
sugar chains. Studies of glycosylated Bence Jones
proteins indicated that this procedure is also applicable to intact
glycoproteins. The behavior of
oligosaccharides isolated from human milk and the urine of patients with
fucosidosis indicated that the
oligosaccharides with Fuc alpha 1----2Gal beta 1----4GlcNAc and Gal beta 1----4(Fuc alpha 1----3)GlcNAc groups interact with the
lectin, but less strongly than complex-type
sugar chains with a fucosylated core. Lacto-N-fucopentaitol II, which has a Gal beta 1----3(Fuc alpha 1----4)GlcNAc group, interacts less strongly than the above two groups with the matrix.
Oligosaccharides with Fuc alpha 1----2Gal beta 1----3GlcNAc and Gal beta 1----4GlcNAc beta 1----3Gal beta 1----4(Fuc alpha 1----3)GlcNAc groups showed almost no interaction with the matrix.