Interaction between Concanavalin A and brain lysosomal acid hydrolases

Abstract

All the five sheep brain lysosomal acid hydrolases tested, namely arylsulphatase A, acid phosphatase, β-N-acetylhexosaminidase, β-galactosidase and β-glucuronidase bind with Concanavalin A and form enzymatically active precipitate. This enzyme-Concanavalin A complex can be dissociated by α-methyl-D-glucoside and the dissociation is pH dependent; except for arylsulphatase A which dissociates maximally at pH 9.0, all other enzymes dissociate maximally at pH 4.0. The enzyme-Concanavalin A complex formation is inhibited by α-methyl-D-glucoside. Using the differential dissociation of the enzyme-Concanavalin A complex, these enzymes have been purified to the extent of 30-180-fold over the soluble lysosomal fraction. The dissociation of the enzyme-Concanavalin A complex and the inhibition of its formation by α-methyl-D-glucoside suggest the glycoprotein nature of the enzymes.