Abstract
MANY carbohydrate-binding proteins, called lectins, purified from plant extracts1, are proving useful for the study of protein-carbohydrate interactions, cell-surface-initiated differentiation of cells and the topography of cell surface constituents1,2. A general method for purification of lectins would markedly augment this work. Affinity chromatography has been successful for purification of some lectins2 although others require conventional chemical fractionation. Purification may be simplified by the availability of commercial carbohydrate polymer adsorbants: for example Sephadex G-503 for concanavalin A and Sepharose 4B for the carbohydrate-binding protein from Dictyostelium discoideum4.
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REITHERMAN, R., ROSEN, S. & BARONDES, S. Lectin purification using formalinised erythrocytes as a general affinity adsorbant. Nature 248, 599–600 (1974). https://doi.org/10.1038/248599a0
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DOI: https://doi.org/10.1038/248599a0
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