Fine sugar specificity of the mistletoe (Viscum album) lectin I |
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Authors: | Henri Debray Jean Montreuil Hartmut Franz |
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Institution: | (1) Laboratoire de Chimie Biologique, Unité Mixte de Recherche du CNRS No. 111, Université des Sciences et Technologies de Lille, F-59655, Villeneuve d'Ascq, France;(2) Institute of Phytochemistry, Universität Witten Herdecke, Berlin, Germany |
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Abstract: | The behaviour ofN-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 unmaskedN-acetyllactosamine sequences. However, substitution of at least one of theN-acetyllactosamine sequences 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 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 1–3Gal sequences. These structures are strongly bound on the lectin column and their elution is obtained with 0.15M galactose in the starting buffer.In memory of Hartmut Franz. |
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Keywords: | mistletoe (Viscum album) lectin I sugar specificity N-acetyllactosamine-type oligosaccharides P1 antigen |
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