title: Electrophoretic study of alpha-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 alpha-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. alpha-D-Galactosidases from both sources interact with immobilized alpha-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 alpha-D-galactosidase and free sugars were calculated.
authors.affiliation: Department of Biochemistry, Charles University, Albertov, Czechoslovakia.
authors.forename: E
authors.initials: E
authors.lastname: Secová
authors.forename: M
authors.initials: M
authors.lastname: Tichá
authors.forename: J
authors.initials: J
authors.lastname: Kocourek
authors.forename: P M
authors.initials: PM
authors.lastname: Dey
mesh_terms: D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005696:Galactosidases / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D037102:Lectins / Q000032:analysis*; D008970:Molecular Weight; D037121:Plant Lectins; D012639:Seeds / Q000201:enzymology*; D013025:Glycine max / Q000201:enzymology*; D000519:alpha-Galactosidase / Q000032:analysis*
chemical_list: D037102:Lectins; D037121:Plant Lectins; D005696:Galactosidases; D000519:alpha-Galactosidase