Studies on sulphatases. 27. The partial purification and properties of the arylsulphatase of the digestive gland of Helix pomatia

Abstract

The arylsulphatase of the digestive gland of Helix pomatia has been partially purified by treatment with manganese chloride followed by fractionation with acetone and ammonium sulphate. The enzyme became progressively more unstable as the purity increased but no other significant changes in the properties of the enzyme occurred during purification, and the final preparation was still exhibiting a shift in pH optimum in the direction of higher pH as the substrate concentration was increased. The observed shift in pH optimum cannot be attributed to the presence of more than one arylsulphatase in the enzyme preparation. The relative behavior of the enzyme towards potassium p-nitrophenyl sulphate and dipotassium 2-hydroxy-5-nitrophenyl sulphate together with the effects of certain inhibitors suggests that the enzyme can be classified as a type II arylsulphatase.