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Studies on lectins 53. affinity electrophoresis in the study of the effect of detergents on the interaction of lectins with carbohydrates



Studies on lectins 53. affinity electrophoresis in the study of the effect of detergents on the interaction of lectins with carbohydrates



Journal of Chromatography 240(1): 43-50



The effect of various types of detergents (Triton X-100, sodium dodecyl sulfate [SDS], cetyltrimethylammonium bromide [CTAB]) on the carbohydrate-binding activity of lectins was investigated by affinity electrophoresis on polyacrylamide gel. The nonionic detergent Triton X-100 (0.5-2%) did not cause dissociation of any of the lectins tested nor did it significantly affect the interaction of lectins with immobilized sugars. Application of the anionic detergent SDS (0.1%) resulted in the rapid dissociation of lectins into subunits. Subunits of none of the lectins studied interacted specifically with carbohydrates. If the dissociation of a lectin was incomplete, the carbohydrate-binding activity of undissociated lectin remained preserved. The cationic detergent CTAB (0.1%) brought about a complete or partial dissociation into subunits. In the presence of CTAB neither subunits nor the undissociated molecules of most of the lectins studied interacted with sugars. Also, in the presence of this detergent, .alpha.-D-glucosyl and .alpha.-D-mannosyl ligands in polyacrylamide copolymers or mannan showed an enhancing effect in the dissociation into subunits of D-mannose-binding lectins (concanavalin A, seed lectins of Pisum sativum, Lens esculenta and Lathyrus sativus).

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