Interaction of a lectin from Psathyrella velutina mushroom with N‐acetylneuraminic acid

FEBS Letters

Ogawa, Haruko¹  Saitoh, Takeshi²  Ueda, Haruko¹  Kojima, Kyoko³ 

[1] Course of Correlational Biosciences, Graduate School of Humanities and Sciences, Ochanomizu University, 2-1-1 Otsuka, Bunkyo-ku, Tokyo 112-8610, Japan;Mushroom Research Institute of Japan, 8-1 Hirai-cho, Kiryuu-shi, Gunma 376-0051, Japan;Department of Chemistry, Faculty of Science, Ochanomizu University, 2-1-1 Otsuka, Bunkyo-ku, Tokyo 112-8610, Japan

关键词: N-acetylneuraminic acid-specific lectin;    Sialoglycoprotein;    Pyridylamino-oligosaccharide;    Biotinylated polymeric sugar-probe;    Mushroom;    Psathyrella velutina;    PVL;    Psathyrella velutina lectin;    PBS;    10 mM phosphate buffer (pH 7.0)-0.13 M NaCl;    GlcNAc5-6;    N-acetylchitooligosaccharides (a mixture of pentamer and hexamer);    BSM;    bovine submaxillary mucin;    NeuAc;    N-acetylneuraminic acid;    LacNAc;    N-acetyllactosamine;    BP-probe;    biotinylated polymeric sugar-probe;    PA-oligosaccharides;    pyridylamino-oligosaccharides;    B-SJA-I;    a galactose-specific lectin from Sophora japonica;   

DOI  :  10.1016/S0014-5793(99)00334-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown