glycine max lectin/phaseolus

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Lectins in fruits having gastrointestinal activity: their participation in the hemagglutinating property of Escherichia coli O157:H7.

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BACKGROUND In fruits with therapeutic properties for antidiarrheal and laxative uses, the presence of lectins may be the bioactive properties that interfere with bacterial adhesion, thought to be competition for glycoside signal sites in the attachment. METHODS This study identifies lectins in crude

Weak protein-protein interactions in lectins: the crystal structure of a vegetative lectin from the legume Dolichos biflorus.

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The legume lectins are widely used as a model system for studying protein-carbohydrate and protein-protein interactions. They exhibit a fascinating quaternary structure variation, which becomes important when they interact with multivalent glycoconjugates, for instance those on cell surfaces.

Rapid release of protease inhibitors from soybeans: immunochemical quantitation and parallels with lectins.

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Specific antisera were prepared against the Bowman-Birk trypsin inhibitor and four other trypsin inhibitors of low molecular weight isolated from soybeans (Glycine max L. cv. Tracy). These antisera were used to detect the presence and amount of the inhibitors in: (a) seeds and protein extracts of

Interaction of lectins with Neisseria gonorrhoeae.

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Fifty-four strains of Neisseria gonorrhoeae were examined for their ability to be agglutinated by various lectins. Wheat germ agglutinin, ricin, soybean lectin, and peanut agglutinin agglutinated all strains tested. Dolichos biflorus, Sophora japonica, Maclura pomifera, Ulex Europaeus, Lens

[Lectins as reagents for the differentiation of serum enzymes. Lectins as reagents, I. (author's transl)].

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Lectins from Canavalia ensiformis, Phaseolus vulgaris, and Triticum vulgare react with arylamidase, alkaline phosphatase, gamma-glutamyltransferase, and cholinesterase of human sera by formation of enzymatically active, mostly insoluble complexes. Arylamidase, alkaline phosphatase, and

Immunochemical and chemical investigations of the structure of glycoprotein fragments obtained from epiglycanin, a glycoprotein at the surface of the TA3-Ha cancer cell.

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The structures of the carbohydrate chains present in fragments of a large-molecular-weight glycoprotein, epiglycanin, cleaved from the surface of viable TA3-Ha murine mammary carcinoma ascites cells and purified by gel filtration, were studied by immunochemical and chemical methods. Inhibitory

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