Carbohydrate-binding properties of an immobilized α- d-galactopyranosyl-binding protein (lectin) from the seeds of Bandeiraea simplicifolia

The α- d-galactopyranosyl-binding lectin from Bandeiraea simplicifolia has been coupled to cyanogen bromide-activated Sepharose 4B. Using this immobilized system, we have been able to study the interaction of the lectin with model carbohydrate—protein conjugates and polysaccharides, and to reaffirm...

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Bibliographic Details
Published in:Carbohydrate research 1976-01, Vol.47 (1), p.91-97
Main Authors: Ross, Timothy T., Hayes, Colleen E., Goldstein, Irwin J.
Format: Article
Language:English
Subjects:
agricultural products
Binding Sites
Chromatography, Affinity
Galactose
Lectins
Plant Lectins
Protein Binding
Seeds - analysis
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Summary:The α- d-galactopyranosyl-binding lectin from Bandeiraea simplicifolia has been coupled to cyanogen bromide-activated Sepharose 4B. Using this immobilized system, we have been able to study the interaction of the lectin with model carbohydrate—protein conjugates and polysaccharides, and to reaffirm this protein's carbohydrate-binding specificity. The opportunity for the isolation of biopolymers containing α- d-galactopyranosyl end-groups is demonstrated by the single step purification of a new galactomannan from the seeds of Cassia alata.
ISSN:0008-6215
1873-426X
DOI:10.1016/S0008-6215(00)83551-X