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
- 4Citations
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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.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021967301888233; http://dx.doi.org/10.1016/s0021-9673(01)88823-3; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0026090348&origin=inward; https://linkinghub.elsevier.com/retrieve/pii/S0021967301888233; https://api.elsevier.com/content/article/PII:S0021967301888233?httpAccept=text/xml; https://api.elsevier.com/content/article/PII:S0021967301888233?httpAccept=text/plain; http://linkinghub.elsevier.com/retrieve/pii/S0021967301888233; http://api.elsevier.com/content/article/PII:S0021967301888233?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0021967301888233?httpAccept=text/plain; http://dx.doi.org/10.1016/s0021-9673%2801%2988823-3; https://dx.doi.org/10.1016/s0021-9673%2801%2988823-3
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