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A lectin, Cyclina sinensis (Gmelin) (CSL), was isolated from hemolymph C. sinensis by ion-exchange on Cellulose DE52 and purified by gel filtration on Sephadex G-100 and HPLC on TSK gel G4000PW XL . SDS-PAGE showed that the CSL protein had a molecular mass of 72kDa, had consisted of 40 and 18kDa subunits. The lectin activity of CSL was Ca 2+ -denpendent. The total carbohydrate content...
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