Interaction of Wheat-Germ Agglutinin with Bacterial Cells and Cell-Wall Polymers
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چکیده
منابع مشابه
The Interaction of Wheat Germ Agglutinin with Sialoglycoproteins
The role of sialic acid in the interaction of sialoglycoproteins with wheat germ agglutinin was investigated by using several well characterized saccharides and sialoglycoconjugates. N-Acetylneuraminic acid and neuramin 2 + 3 lactose, in addition to N-acetyl-Dglucosamine and its fil-+ 4 oligomers were found to be inhibitors of wheat germ agglutinin-induced hemagglutination. Neuraminic acid-/?-m...
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Procedures for the isolation, purification, and crystallization of wheat germ agglutinin are described. The agglutinin was purified 184-fold to homogeneity from commercial wheat germ lipase. A molecular weight of 23,500 was estimated for the protein by means of sedimentation equilibrium and sodium dodecyl sulfate gel electrophoresis. The agghxtinin is a glycoprotein. Amino acid and carbohydrate...
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In this study, we revealed that the lectin wheat germ agglutinin (WGA) and its specific binding sugars, N-acetylneuraminic acid (NeuAc) and Nacetylglucosamine (GlcNAc), inhibited mating pair formation in Paramecium caudatum. The concentrations that caused 50% inhibition (IC50) were 17 nM, 3 mM and 30 mM, respectively. Using FITCWGA, it was shown fluorescence-cytochemically that WGA bound to the...
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The effects of wheat germ agglutinin on Drosophila embryonic cell lines growing on cover-glasses was examined by scanning electron microscopy. At low concentrations of the lectin (5-10 mug/ml), cells spread against the glass surface and fused to form syncytia. At high concentration, damage to the cell surface was evidenced as extensive membrane shrivelling and loss of surface microfilaments. Fu...
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Two Chinese hamster ovary (CHO) cell mutants selected for resistance to wheat germ agglutinin (WGA) have been shown to exhibit defective sialylation of membrane glycoproteins and a membrane glycolipid, GM3. The mutants (termed WgaRII and WgaRIII) have been previously shown to belong to different genetic complementation groups and to exhibit different WGA-binding abilities. These mutants and a W...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1975
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1975.tb02158.x