Electrophoretic study of α- d-galactosidases from seeds of glycine soja and vigna radiata possessing erythroagglutinating activity

Abstract

Polyacrylamide gel electrophoresis in an acidic buffer system was used to study the electrophoretic behaviour of two forms of α- d-galactosidase from seeds of soy bean (Glycine soja) and mung bean (Vigna radiata). The interaction of the enzymes with saccharides was monitored by affinity electrophoresis; for the preparation of affinity gels, water-soluble O-glycosyl polyacrylamide copolymers and polysaccharides were used. α- d-Galactosidases from both sources interact with immobilized α- d-galactosyl residues. On the basis of the results of affinity electrophoresis performed in the presence of various free sugars, dissociation constants for the complexes between α- d-galactosidase and free sugars were calculated.