The characterization of a thermostable activator of β-D-glucosidase in normal human saliva

Abstract

The existence of thermostable activators of β-D-glucosidase (EC 3.2.1.21) in Gaucher tissues is known. We demonstrate the presence of a thermostable factor in normal human saliva which activates the β3-d-glucosidase of saliva. The activator is specific for β-glucosidase. It is dialysable and susceptible to pronase digestion. Sephadex G-25 gel filtration indicates that the activator is of low molecular weight, and polyacrylamide gel electrophoresis shows the low molecular weight fraction to migrate as two closely moving protein bands. A major proportion of the activator does not bind to concanavalin A-Sepharose. The activator appears to act by binding to or modifying the salivary β-glucosidase in a time-dependent manner.