Farooqui A A, Hanson W L
Biochem J. 1987 Feb 15;242(1):97-102. doi: 10.1042/bj2420097.
Chicken caecal arylsulphatase was purified 700-fold by (NH4)2SO4 fractionation, concanavalin A-Sepharose and cyclic AMP-Sepharose chromatographies. The purified enzyme was a glycoprotein of Mr 97,000. It hydrolysed p-nitrocatechol sulphate, cerebroside 3-sulphate and ascorbic acid 2-sulphate and was strongly inhibited by Na2SO4 (Ki = 50 microM) and Na3PO4 (Ki = 20 microM). Arylsulphatase from Eimeria tenella sporozoites was purified 28-fold by (NH4)2SO4 fractionation. Arylsulphatase of E. tenella sporozoites was not a glycoprotein. It had an Mr of 49,000. It was inhibited by Na2SO4 (Ki = 300 microM), sodium phosphate (Ki = 90 microM) and heparin. It hydrolysed ascorbic acid 2-sulphate, but cerebroside 3-sulphate was not desulphated. The kinetic parameters of chicken caecal arylsulphatase were different from those of the E. tenella enzyme.
鸡盲肠芳基硫酸酯酶通过硫酸铵分级分离、伴刀豆球蛋白A-琼脂糖凝胶和环磷酸腺苷-琼脂糖凝胶色谱法纯化了700倍。纯化后的酶是一种分子量为97,000的糖蛋白。它能水解对硝基儿茶酚硫酸酯、脑苷脂3-硫酸酯和抗坏血酸2-硫酸酯,并受到硫酸钠(Ki = 50 μM)和磷酸钠(Ki = 20 μM)的强烈抑制。柔嫩艾美耳球虫子孢子的芳基硫酸酯酶通过硫酸铵分级分离纯化了28倍。柔嫩艾美耳球虫子孢子的芳基硫酸酯酶不是糖蛋白。其分子量为49,000。它受到硫酸钠(Ki = 300 μM)、磷酸钠(Ki = 90 μM)和肝素的抑制。它能水解抗坏血酸2-硫酸酯,但不能使脑苷脂3-硫酸酯脱硫。鸡盲肠芳基硫酸酯酶的动力学参数与柔嫩艾美耳球虫酶的不同。