Temperature effect on affinity chromatography of two lectins from the seeds of Ricinus communis

Binding of Ricinus communis agglutinin (RCA 120) to carbohydrate receptors of human lymphocytes and erythrocytes is enth~pically driven. As in the case of simple saccharides, the AS cont~bution is always unfavorable to the interaction. This result is different from that observed for other lectins and might indicate that hydrophobic interactions do not play a dominant role in binding of RCA 120 to cell surfaces. Ricinus communis agglutininHuman lymphocyte Lectin-cell surface interaction

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Crystallographic characterization of a principal non-toxic lectin from seeds of Ricinus communis

Wei

Koh

1978

Journal of Molecular Biology

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Temperature effect on affinity chromatography of two lectins from the seeds of Ricinus communis

Cited by 7 publications

References 8 publications

Binding of Concanavalin A to Ricinus communis agglutinin and its implication in cell‐surface labeling studies

Binding of Concanavalin A to Ricinus communis agglutinin and its implication in cell‐surface labeling studies

Nature of the interaction between Ricinus communis agglutinin and blood cells

Crystallographic characterization of a principal non-toxic lectin from seeds of Ricinus communis

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