Steroid sulphatase, arylsulphatase and β-glucuronidase in the mollusca

Abstract

Acetone-dried powders prepared from 13 species of molluscs have been tested for steroid-sulfatase activity with the sulfates of dehydroepiandrosterone, androsterone and etiocholanolone as substrates. Three species (Helix pomatia, Buccinum undatum and Nassarius reticulatus) possess activity towards both dehydroepiandrosterone sulfate and etiocholanolone sulfate, whereas in 4 species (Patella vulgata, Littorina littorea, Patina pellucida and Nucella lapillus) activity towards only dehydroepiandrosterone sulfate was found. Steroid-sulfatase activity was not detected in 6 species. No enzyme capable of hydrolyzing androsterone sulfate was found in any of the animals tested; therefore complete enzymic hydrolysis of urinary steroid conjugates cannot be achieved with enzyme preparations from these molluscs. [beta]-Glucuronidase and arylsulfatase activity are widely distributed in the Mollusca, but the activities of these enzymes are not related to the activity of steroid sulfatase.