Fine sugar specificity of the mistletoe (VISCUM ALBUM) lectin I

Journal/Book: Glycoconjugate J. 11, 550-557. 1994;

Abstract: The behaviour of N-acetyllactosamine-type oligosaccharides andglycopeptides on a column of mistletoe lectin I (MLI) immobilized onSepharose 4B was examined. The immobilized lectin does not show anyaffinity 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-acetyllactosaminesequences by sialic acid residues, either at O-3 or O-6 of galactose,slightly enhances the affinity of the lectin. Such sialylatedN-glycosylpeptides or oligosaccharides are eluted from the lectin columnby the starting buffer as retarded fractions. Surprisingly, the affinityof the immobilized MLI is higher for P1 antigen-containing glycopeptideisolated from turtle-dove ovomucoid and for glycopeptides from bovinethyroglobulin containing terminal non-reducing Gal alpha 1-3Galsequences. These structures are strongly bound on the lectin column andtheir elution is obtained with 0.15 M galactose in the starting buffer.Author.

Keyword(s): BINDING-SITES

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