Electrophoretic study of α- d-mannosidase and α- d-galactosidase from dry seeds of Pisum sativum

Abstract

Polyacrylamide gel electrophoresis in an acidic buffer system was used to study the electrophoretic behaviour of one form of α- d-mannosidase and the three forms of α- d-galactosidase from pea seeds Pisum sativum. Affinity electrophoresis was used to study the interaction of the studied enzymes with saccharides; water-soluble O-glycosyl polyacrylamide copolymers and polysaccharides were used for the preparation of affinity gels. Multiple forms of α- d-galactosidase were shown to inteact with immobilized α- d-galactosyl residues, whereas no interaction of α- d-mannosidase with immobilized α- d-mannosyl residues or with mannan, dextran or glycogen was observed. On the basis of the results of affinity electrophoresis of α- d-galactosidase, dissociation constants of complexes between the enzyme and immobilized α- d-galactosyl residues were calculated.