Interaction of a lectin from Psathyrella velutina mushroom with N-acetylneuraminic acid.
A lectin from the fruiting body of Psathyrella velutina has been used as a specific probe for non-reducing terminal N-acetylglucosamine residues. We reveal in this report that P. velutina lectin recognizes a non-reducing terminal N-acetylneuraminic acid residue in glycoproteins and oligosaccharides. Binding of biotinyl P. velutina lectin to N-acetylneuraminic acid residues was prevented by desialylation of glycoconjugates and was distinguished from the binding to N-acetylglucosamine. Sialooligosaccharides were retarded or bound and eluted with N-acetylglucosamine on a P. velutina lectin column, being differentiated from each other and also from the oligosaccharides with non-reducing terminal N-acetylglucosamine which bound more strongly to the column.
Ueda
H
H
Graduate School of Humanities and Sciences, Ochanomizu University, Tokyo, Japan.
Kojima
K
K
Saitoh
T
T
Ogawa
H
H
D001487:Basidiomycota / Q000378:metabolism*; D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity; D037102:Lectins / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D019158:N-Acetylneuraminic Acid / Q000378:metabolism*; D009844:Oligosaccharides / Q000378:metabolism; D012685:Sepharose / Q000378:metabolism; D012795:Sialoglycoproteins / Q000378:metabolism
D037102:Lectins; D009844:Oligosaccharides; D012795:Sialoglycoproteins; D012685:Sepharose; D019158:N-Acetylneuraminic Acid