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  • Title: Fine sugar specificity of the mistletoe (Viscum album) lectin I.
    Author: Debray H, Montreuil J, Franz H.
    Journal: Glycoconj J; 1994 Dec; 11(6):550-7. PubMed ID: 7696858.
    Abstract:
    The behaviour of N-acetyllactosamine-type oligosaccharides and glycopeptides on a column of mistletoe lectin I (MLI) immobilized on Sepharose 4B was examined. The immobilized lectin does not show any affinity for asialo-N-glycosylpeptides and related oligosaccharides, which possess one to four unmasked N-acetyllactosamine sequences. However, substitution of at least one of the N-acetyllactosamine sequences by sialic acid residues, either at O-3 or O-6 of galactose, slightly enhances the affinity of the lectin. Such sialylated N-glycosylpeptides or oligosaccharides are eluted from the lectin column by the starting buffer as retarded fractions. Surprisingly, the affinity of the immobilized MLI is higher for P1 antigen-containing glycopeptide isolated from turtle-dove ovomucoid and for glycopeptides from bovine thyroglobulin containing terminal non-reducing Gal alpha 1-3Gal sequences. These structures are strongly bound on the lectin column and their elution is obtained with 0.15 M galactose in the starting buffer.
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