Electrophoretic study of alpha-D-galactosidases from seeds of Glycine soja and Vigna radiata possessing erythroagglutinating activity

Jazyk angličtina Země Nizozemsko Médium print

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/pmid02836454

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.

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