Abstract
The interaction of wheat germ agglutinin with sialoglycoproteins. The role of sialic acid.
Highlights
State University, The role of sialic acid in the interaction of sialoglycoproteins with wheat germ agglutinin was investigated by using several well characterized saccharides and sialoglycoconjugates
The results suggest that the binding of a glycoprotein to a wheat germ agglutinin-Sepharose column may be influenced both by the density of the binding sugar residues
Interaction of labeled glycoproteins with diff erentpreparations of wheat germ agglutinin (WGA)-Sepharose were labeled on the protein by acetylation; sialoglycoproteins were labeled on sialic
Summary
State University, The role of sialic acid in the interaction of sialoglycoproteins with wheat germ agglutinin was investigated by using several well characterized saccharides and sialoglycoconjugates. Glucosamine and its fil-+ 4 oligomers were found to be inhibitors of wheat germ agglutinin-induced hemagglutination. Neuraminic acid-/?-methyl ketoside, N-glycolylneuraminic acid and several other acidic sugars were noninhibitors Both glycophorin and al-acid glycoprotein were excellent inhibitors, whereas the corresponding asialo compounds were either very poor or noninhibitors. The results of double diffusion experiments, in which the ability of the glycoconjugates to form precipitin line with wheat germ agglutinin was tested, were in agreement with the agglutination inhibition data. Affinity chromatography of labeled glycoconjugates on wheat germ agglutinin-Sepharose this lectin. The results suggest that the binding of a glycoprotein to a wheat germ agglutinin-Sepharose column may be influenced both by the density of the binding sugar residues The cells interacted irreversibly with wheat germ agglutinin-Sepharose this binding was partially lost on treatment of the cells with neuraminidase
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