van der Pal R H, Klein W, van Golde L M, Lopes-Cardozo M
Laboratory of Veterinary Biochemistry, Utrecht University, The Netherlands.
Biochim Biophys Acta. 1991 Feb 5;1081(3):315-20. doi: 10.1016/0005-2760(91)90288-s.
Arylsulfatases A (EC 3.1.6.1) and B (EC 3.1.6.12) are lysosomal enzymes that can remove sulfate groups from sulfatides and sulfo-glycosaminoglycans, respectively. The activities of these enzymes in cerebral cortex and in spinal cord of developing rat pups were measured. The tissues were homogenized and the arylsulfatases A and B in the soluble fraction were separated from each other by anion exchange chromatography on DE-52 cellulose. Subsequently, the enzyme activities were assayed with p-nitrocatechol sulfate as substrate at 37 degrees C and pH 5.6. We observed a developmental profile of arylsulfatase A, similar to that previously reported for cerebroside sulfatase (EC 3.1.6.8; (Van der Pal et al. (1990) Biochim. Biophys. Acta 1043, 91-96]. The activity of arylsulfatase A increased gradually during development, whereas arylsulfatase B rose more steeply, peaked around day 15 and declined thereafter. As a consequence the ratio between B and A forms of arylsulfatase dropped from about 4 in 1-week-old pups to 2.2 (cortex) and 0.7 (cord) in 7-week-old rat pups.
芳基硫酸酯酶A（EC 3.1.6.1）和芳基硫酸酯酶B（EC 3.1.6.12）是溶酶体酶，分别可从硫苷脂和硫代糖胺聚糖中去除硫酸基团。测定了这些酶在发育中幼鼠大脑皮层和脊髓中的活性。将组织匀浆，通过在DE - 52纤维素上进行阴离子交换色谱法，将可溶性部分中的芳基硫酸酯酶A和B彼此分离。随后，以对硝基儿茶酚硫酸酯为底物，在37℃和pH 5.6条件下测定酶活性。我们观察到芳基硫酸酯酶A的发育情况，与先前报道的脑苷脂硫酸酯酶（EC 3.1.6.8；（范德帕尔等人（1990年）《生物化学与生物物理学报》1043，91 - 96））相似。芳基硫酸酯酶A的活性在发育过程中逐渐增加，而芳基硫酸酯酶B上升更为陡峭，在第15天左右达到峰值，此后下降。因此，芳基硫酸酯酶B与A形式的比例从1周龄幼鼠的约4降至7周龄幼鼠大脑皮层的2.2和脊髓的0.7。
