Purification of an acid α-glucosidase by dextran-gel filtration

Abstract
The behavior of rat liver [alpha]-glucosidases on dextran gel (Sephadex G-100) columns was studied. A "retardation" of an acid [alpha]-glucosidase activity was observed. This activity was identified as lysosome [alpha]-(l[long dash])4)-glucosidase. A single gel-filtration step resulted in a 700-fold purification of the enzyme. The same technique was also used to purify the acid [alpha]-glucosidase of human kidney. The acid [alpha]-glucosidases of both tissues show very similar pH optima when tested with maltose or glycogen as substrate.