The binding of human liver acid beta-galactosidase to wheat-germ lectin is influenced by aggregation state of the enzyme.

Abstract

At low ionic strength and pH 6.0 human liver acid beta-galactosidase exists in two aggregation states, monomeric and multimeric. These species can be separated on wheat-germ lectin-Sepharose, Cellogel electrophoresis and gel filtration on Sephadex G-200, and are not normally interconvertible. On re-application of either form to wheat-germ lectin-Sepharose the equilibrium is re-established and the two forms are interconverted.