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

Journal of Chromatography A, ISSN: 0021-9673, Vol: 540, Issue: C, Page: 365-372
1991
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Article Description

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.

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