Selective loss of wheat germ agglutinin binding to agglutinin-resistant mutants of Chinese hamster ovary cells.
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چکیده
منابع مشابه
Differential involvement of cell surface sialic acid residues in wheat germ agglutinin binding to parental and wheat germ agglutinin-resistant Chinese hamster ovary cells
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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The binding of [125I]wheat germ agglutinin ([125I]WGA) of high specific activity to Chinese hamster ovary (CHO) cells has been examined over a millionfold range of WGA concentrations and correlated with the phenomena of agglutination and capping by WGA. Analysis of the binding data by the method of Scatchard gives a complex curve indicative of positive cooperativity amongst high-affinity bindin...
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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...
متن کاملStructural basis of multivalent binding to wheat germ agglutinin.
The inhibition of carbohydrate-protein interactions by tailored multivalent ligands is a powerful strategy for the treatment of many human diseases. Crucial for the success of this approach is an understanding of the molecular mechanisms as to how a binding enhancement of a multivalent ligand is achieved. We have synthesized a series of multivalent N-acetylglucosamine (GlcNAc) derivatives and s...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1977
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.74.11.5056