Studies on the interaction of immobilized lectin from Ricinus communis with a simple sugar and a polysaccharide

Surolia, Avadhesha ; Ahmad, Ateeq ; Bachhawat, B. K. (1974) Studies on the interaction of immobilized lectin from Ricinus communis with a simple sugar and a polysaccharide Biochimica et Biophysica Acta (BBA) - Protein Structure, 371 (2). pp. 491-500. ISSN 0005-2795

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000527...

Related URL: http://dx.doi.org/10.1016/0005-2795(74)90045-2

Abstract

A glycoprotein lectin from Ricinus communis (RCA1) has been immobilized using concanavalin A. The concanavalin A-immobilized RCA1 retains its sugar binding properties. The number of binding sites (n) and the apparent association constant (Ka) for lactose are not altered on immobilization. This is the first report which indicates that the carbohydrate moieties of a lectin may not be essential for its sugar binding property. The polysaccharide (guar gum) binding can be measured much more effectively by the immobilized RCA1 as compared to free RCA1. The pH optimum for the binding of guar gum to RCA1 is broader for the immobilized RCA1 as compared to free RCA1. The immobilized RCA1 shows considerable stability to thermal inactivation and urea denaturation as compared to free RCA1. We suggest that the technique of immobilization, where the functional group of a glycoprotein lectin remains available for its biological activity, could prove an important tool for the study of receptor hormone and antibody-antigen interactions.

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