Studies on the function of the activator of sulphatase A

Abstract

The activator of sulphatase A is necessary for the enzymic degradation of sulphatides to cerebrosides at ionic concentrations in the physiological range (1). Activation is probably due to the reversible formation of a one-to-one complex between activator and sulphatides (1,2). Formation of this complex is partly inhibited by cerebrosides due to competitive binding (2), as well as by phospholipids (e.g. lecithin or phosphatidylserine). Inhibition of the complex formation between activator and sulphatides by cerebrosides and phosphatidyl-serine depends on the concentration of the lipids and is of the same order of magnitude as the inhibition (by these lipids) of the enzymic degradation of sulphatides in the presence of activator (1). Moreover the degradation rate of sulphatides increases with the concentration of activator-sulphatide complex in the reaction mixture (1) indicating that the activator-sulphatide complex is the substrate for the enzyme in the degradation of sulphatides by sulphatase A.