The use of concanavalin A in the purification or separation of multiple forms of brain hydrolases

Abstract

Concanavalin A bound to Sepharose has been used for the purification of brain β-galactosidase, α -L-fucosidase, α-D-mannosidase, arylsulphatase and α- glucuronidase. Several factors viz pH, temperature and concentration of α-methyl glucoside influenced the binding and elution of these enzymes. A lysosomal acid α- mannosidase and a cytosolic neutral mannosidase were separable by concanavalin ASepharose chromatography. Similarly lysosomal and microsomal β-glucuronidases were separable using gradient elution with α-methyl glucoside. The results indicate the usefulness of this lectin for the isolation of wide variety of enzymes under specified experimental conditions.