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Interaction of a lectin from Psathyrella velutina mushroom with N ‐acetylneuraminic acid
Author(s) -
Ueda Haruko,
Kojima Kyoko,
Saitoh Takeshi,
Ogawa Haruko
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00334-8
Subject(s) - lectin , glycoconjugate , n acetylneuraminic acid , biochemistry , glycoprotein , chemistry , acetylglucosamine , n acetylglucosamine , sialic acid , residue (chemistry) , glycan , mushroom , ficolin , biology , mannan binding lectin , enzyme , food science
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.