Glycosulphatase: observations on the activity of partially purified preparations towards the sulphate esters of certain monosaccharides and steroids

Publisher Website
Google Scholar
Abstract
The glycosulphatase of the digestive organs of the common periwinkle, Littorina littorea, has been purified 20-fold. Chondroitinase, [beta]-glucuronidase and [beta]-N acetylglucosaminidase,. which are also present in aqueous extracts of the digestive organs, are eliminated or greatly decreased in concentration during the purification procedure. The potassium salts of the 3-0 sulphate and 6-O-sulphate esters of glucose and the 6-O sulphate esters of galactose have been used as substrates for glycosulphatase. The enzyme shows greatest affinity and activity towards glucose 6-O-sulphate. The final enzyme preparation, which also contains appreciable amounts of arylsulphatase and 3 [beta]-steroid sulphatase, is able to hydrolyze sodium cortisone 21-sulphate. Mixed-substrate experiments provide no support for the suggestion that glycosulphatase is the enzyme responsible for the hydrolysis of cortisone 21-sulphate. Preparations of the digestive juice of Helix pomatia. when diluted 40-fold, show little or no activity towards glucose 6-O-sulphate and dehydroisoandrosterone sulphate but are strongly active towards cortisone 21-sulphate.