Studies on lectins. LVIII. Sugar-binding properties, as determined by affinity electrophoresis, of alpha-D-galactosidases from Vicia faba seeds possessing erythroagglutinating activity.
The interaction of alpha-D-galactosidases from Vicia faba seeds with saccharides was studied by means of affinity electrophoresis on polyacrylamide gel in an acidic buffer system. For the preparation of affinity gels, water-soluble O-glycosyl polyacrylamide copolymers and polysaccharides were used. alpha-D-Galactosidases interact with immobilized O-alpha-D-galactosyl residues and glycogen, but no interaction was observed with immobilized O-alpha-D-mannosyl residues. On the basis of the results of affinity electrophoresis performed in the presence of various free sugars, dissociation constants of the various alpha-D-galactosidase-free sugar complexes were calculated.
D000371:Agglutination / Q000187:drug effects; D002241:Carbohydrates / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D005696:Galactosidases / Q000302:isolation & purification*; D006801:Humans; D066298:In Vitro Techniques; D037102:Lectins / Q000032:analysis / Q000494:pharmacology*; D037121:Plant Lectins; D011506:Proteins / Q000032:analysis; D012639:Seeds / Q000032:analysis*; D000519:alpha-Galactosidase / Q000302:isolation & purification* / Q000494:pharmacology
D002241:Carbohydrates; D037102:Lectins; D037121:Plant Lectins; D011506:Proteins; D005696:Galactosidases; D000519:alpha-Galactosidase