Factors affecting the molecular structure and the agglutinating ability of concanavalin A and other lectins
Ultracentrifugation analyses were performed on lectins under varying conditions of pH, ionic strength and temperature. It has been demonstrated that the phytohemagglutinin from Phaseolus vulgaris, the wheat germ agglutinin and the soybean agglutinin are stable when these parameters are varied, whereas the concanavalin A molecule exhibits a striking reversible dimer-tetramer transition with variation in pH (from 6.0 to 7.2) and temperature (from 4 degrees up to 37 degrees C). It has also been demonstrated that, in agglutination experiments undertaken at different temperatures, cells do eventually aggregate with the first three lectins provided that incubation time is sufficient, whereas the concanavalin-A-induced agglutination was previously found to be temperature-sensitive. These results strongly suggest that the effect of temperature on agglutination by lectins may essentially be due to a structural transition of the lectin itself and nott only to modification of cell surface properties.
Protein-carbohydrate interaction. VII. Physical and chemical studies on concanavalin A, the hemagglutinin of the jack bean
The use of protein A and concanavalin A to examine the possible role of the carbohydrate of IgG in the binding of Clq
Quantitative analysis of multivalent ligand presentation on gold glyconanoparticles and the impact on lectin binding
Photo- and biophysical studies of lectin-conjugated fluorescent nanoparticles: reduced sensitivity in high density assays
Binding of 4-methylumbelliferyl alpha-D-mannopyranoside to tetrameric concanavalin A Fluorescence temperature-jump relaxation study
Binding of 4-methylumbelliferyl alpha-D-mannopyranoside to tetrameric and unmodified or derivatized dimeric concanavalin A: equilibrium studies
Equilibrium and kinetic studies of the binding of Lens culinaris lectin to rabbit erythrocytes by a quantitative fluorometric method
Lectins for the detection of IgM antibodies to T. gondii in the diagnosis of acute toxoplasmosis by immunofluorescence test
The binding of 125I-labeled concanavalin A to the cell surface of rabbit peritoneal polymorphonuclear leucocytes
The effect of temperature on the agglutinability by lectins of liposomes prepared from total lipids of erythrocytes
Fabrication of highly stable glyco-gold nanoparticles and development of a glyco-gold nanoparticle-based oriented immobilized antibody microarray for lectin (GOAL) assay
Canavalia ensiformis-derived lectin inhibits biofilm formation of enterohemorrhagic Escherichia coli and Listeria monocytogenes
Binding of multivalent carbohydrates to concanavalin A and Dioclea grandiflora lectin. Thermodynamic analysis of the "multivalency effect"
Discrimination of glycoproteins via two-color laser-induced fluorescence detection coupled with postcolumn derivatization in capillary electrophoresis
"Tuning aggregative versus non-aggregative lectin binding with glycosylated nanoparticles by the nature of the polymer ligand".
Antibody-mediated agglutination is the clumping of cells in the presence of antibody, which binds multiple cells together. This enhances the clearance of pathogens. Find the latest research on antibody-mediated agglutination here.