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vicia cracca/carbohydrate
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5 resultados
Antigenic similarities both inside and outside the carbohydrate-binding sites of two-chain and one-chain leguminous lectins.
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Antibodies were made against the two-chain lectin Lath-O from the seeds of Lathyrus odoratus as well as its isolated light (alpha) and heavy (beta) chains. These antibodies were used to antigenically compare the Lath-O with other two-chain lectins like Lath-S, lentil and Vicia cracca glc specific
Studies with lectins on the surface carbohydrate structures of mycoplasma membranes.
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The surface carbohydrate structures on the cell membranes of various mycoplasma species have been investigated by using lectins, which are sugar-specific proteins. Carbohydrate structures presumably bound to glycolipids, with both galactose and glucose units, were found to be exposed on the surface
Blood-group A and B determinants are located in different polyglycosyl peptides isolated from human erythrocytes of blood-group AB.
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The distribution of blood-group A and B determinants was studied by isolating blood-group ABH-active polyglycosyl peptides from delipidated human blood-group AB erythrocyte membranes after extensive digestion with pronase followed by chromatography on Bandeiraea simplicifolia I (BsI) lectin coupled
Lectins as markers for blood grouping.
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Lectins are unique proteins of varying biological importance. They are characterized by specific binding to carbohydrate residues, whether monosaccharides, disaccharides or polysaccharides. The sugar heads on the surface of the erythrocyte specify the different blood groups. Lectins, as an antigenic
Studies on lectins. XXXVI. Properties of some lectins prepared by affinity chromatography on O-glycosyl polyacrylamide gels.
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A number of lectins has been purified by affinity chromatography on O-glycosyl polyacrylamide gels. The lectins isolated (and the particular sugar ligands used in the affinity carriers) are as follows: Anguilla anguilla, serum (alpha-L-fucosyl-), Vicia cracca, seeds; Phaseolus lunatus, seeds;
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