Electrophoretic study of alpha-D-galactosidases from seeds of Glycine soja and Vigna radiata possessing erythroagglutinating activity.
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.
Secová
E
E
Department of Biochemistry, Charles University, Albertov, Czechoslovakia.
Tichá
M
M
Kocourek
J
J
Dey
P M
PM
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*
D037102:Lectins; D037121:Plant Lectins; D005696:Galactosidases; D000519:alpha-Galactosidase