Roy A B, Turner J
Biochim Biophys Acta. 1982 Jun 4;704(2):366-73. doi: 10.1016/0167-4838(82)90167-4.
The rhodizonic acid method for the determination of SO2-4 has been used to investigate the glycosulphatase activity of the sulphatase A (aryl-sulphate sulphohydrolase, EC 3.1.6.1) of ox liver. Sulphatase A hydrolyses D-glucopyranose and D-galactopyranose 2-, 3-, 4- and 6-sulphates: glucose sulphates are hydrolysed more rapidly than galactose sulphates and the 3-sulphates more rapidly than the other isomers. 2-Acetamido-2-deoxyglucopyranose 6-sulphate is not hydrolysed, nor is 2,3,4,6-tetra-O-acetyl-beta-D-glucopyranose 1-sulphate. Sulphate is a competitive inhibitor of the glycosulphatase activity. Hydrolysis proceeds through fission of the O-S bond. Evidence is given that the hydrolysis of glucose 3-sulphate is accompanied by the formation of substrate-modified sulphatase A, although this has not been isolated. Sulphatase A has no detectable alkylsulphatase activity.
已采用测定硫酸根离子的玫棕酸法来研究牛肝中硫酸酯酶A（芳基硫酸酯硫酸水解酶，EC 3.1.6.1）的糖硫酸酯酶活性。硫酸酯酶A可水解D-吡喃葡萄糖和D-吡喃半乳糖的2-、3-、4-和6-硫酸盐：葡萄糖硫酸盐的水解速度比半乳糖硫酸盐快，3-硫酸盐的水解速度比其他异构体快。2-乙酰氨基-2-脱氧吡喃葡萄糖6-硫酸盐不被水解，2,3,4,6-四-O-乙酰基-β-D-吡喃葡萄糖1-硫酸盐也不被水解。硫酸根是糖硫酸酯酶活性的竞争性抑制剂。水解通过O-S键的断裂进行。有证据表明，葡萄糖3-硫酸盐的水解伴随着底物修饰的硫酸酯酶A的形成，尽管尚未将其分离出来。硫酸酯酶A没有可检测到的烷基硫酸酯酶活性。
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