Fine sugar specificity of the mistletoe (Viscum album) lectin I.
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.
Debray
H
H
Laboratoire de Chimie Biologique, Unité Mixte de Recherche du CNRS No. 111, Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France.
Montreuil
J
J
Franz
H
H
D001665:Binding Sites; D050260:Carbohydrate Metabolism; D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity; D037102:Lectins / Q000378:metabolism*; D014784:Mistletoe / Q000378:metabolism*; D008969:Molecular Sequence Data; D037121:Plant Lectins; D028321:Plant Preparations; D010940:Plant Proteins; D010946:Plants, Medicinal; D054790:Ribosome Inactivating Proteins, Type 2; D014118:Toxins, Biological / Q000302:isolation & purification / Q000378:metabolism*
D037102:Lectins; D037121:Plant Lectins; D028321:Plant Preparations; D010940:Plant Proteins; D054790:Ribosome Inactivating Proteins, Type 2; D014118:Toxins, Biological; C009674:ribosome inactivating protein, Viscum