The Binding of Sulphatase by Rat-Liver Particles as Compared to That of Acid Phosphatase

Abstract

One of the sulphatases of rat liver, like acid phosphatase, is enclosed within cytoplasmic granules. The two enzymes are released from these granules in similar proportions by various treatments.

Mucopolysaccharidoses and mucolipidoses

“…Arylsulphatase A, a lysosomal enzyme (Viala and Gianetto, 1955), is practically inactive in brain, liver, kidney, urine (Austin, 1965), and leucocytes (Van Hoof, 1972). The enzyme protein, however, can be demonstrated immunologically (Austin, 1973a and b).…”

The Synthesis and Hydrolysis of Sulfate Esters

“…The aryl sulfatases A and B of mammalian livers occur in both the mitochondria1 and microsomal fractions of the usual sucrose homogenate (47,116,126,159) and, unlike the corresponding aryl sulfatases C, can readily be obtained in true solution either from the fresh tissue or from an acetone powder (117). These enzymes apparently occur mainly in the lysosomes (126,159), but the presence of small amounts in the microsomes cannot be completely excluded since aryl sulfatases A and B are normally present in the insoluble preparations of the purely niicrosomal aryl sulfatase C (122,126).…”

“…These enzymes apparently occur mainly in the lysosomes (126,159), but the presence of small amounts in the microsomes cannot be completely excluded since aryl sulfatases A and B are normally present in the insoluble preparations of the purely niicrosomal aryl sulfatase C (122,126). This could, of course, be due to secondary absorption of the solubilized lysosomal enzymes onto the microsomes.…”

The metabolism of dipotassium 2-hydroxy-5-nitrophenyl [35S]sulphate, a substrate for lysosomal arylsulphatases A and B

“…Mammalian tissues contain three arylsulphatase enzymes (aryl sulphate sulphohydrolases, EC 3.1.6.1), designated A, B and C, that can hydrolyse aryl sulphate esters (Dodgson, Spencer & Thomas, 1955a). Though the specificities of the enzymes are not yet absolutely defined it is clear that arylsulphatases A and B, which are lysosomal in origin (Viala & Gianetto, 1955), show high activity and affinity for such substrates as dipotassium 2-hydroxy-5-nitrophenyl sulphate (nitrocatechol sulphate), and comparatively low activity towards simpler aryl sulphates such as potassium p-acetylphenyl sulphate and potassium p-nitrophenyl sulphate. In contrast, arylsulphatase C, a microsomal enzyme, is particularly active towards these simpler aryl sulphates (see Dodgson, Spencer & Thomas, 1954).…”