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Abstract
Interaction of acetylcholinesterase (AChE) of human erythrocyte membranes with wheat germ lectin, Concanavalin A, Lens Culinaris lectin and phytohaemagglutinin is described. In solutions containing Triton X 100, only Wheat Germ lectin showed significant binding with AChE. Sepharose-immobilized Wheat Germ lectin bound AChE significantly more than Concanavalin A. This interaction was used for partial purification of the enzyme.