The enzymic hydrolysis of steroid conjugates. 1. Sulphatase and β-glucuronidase activity of molluscan extracts

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Abstract
Methods are described for the preparation and purification from molluscs of a sulfatase capable of hydrolyzing the Na salt of dehydroepiandrosterone sulfate, and a [beta]-glucuronidase enzyme system. Properties of the sulfatase and a method of assay are described. The sulfatase had no action on androsterone sulfate. Some properties of the [beta]-glucuronidase were described with respect to its action on borneol glucuronide and pregnanediol glucuronide. Evidence for the existence of a dialyzable sulfatase inhibitor in the extracts is presented. An irreversible inactivation of the sulfatase at pH values over 9 and of the [beta]-glucuronidase at pH below 3 was demonstrated. The specificity of the sulfatase is a limiting factor in the application to the hydrolysis of urinary steroid conjugates.