人肝艾杜糖醛酸硫酸酯酶的纯化及某些性质
Purification and some properties of human liver iduronate sulfatase.
作者信息
Yutaka T, Fluharty A L, Stevens R L, Kihara H
出版信息
J Biochem. 1982 Feb;91(2):433-41. doi: 10.1093/oxfordjournals.jbchem.a133715.
Iduronate sulfatase was purified from human liver for an investigation of the degradative pathway of dermatan sulfate. An overall 80-fold purification was achieved and, more importantly, the preparation was free of alpha-L-iduronidase, beta-glucuronidase, N-acetylgalactosamine 4-sulfate sulfatase (arylsulfatase B) and highly enriched in beta-N-acetylhexosaminidase. The liver enzyme appeared to be composed of several molecular species. The enzyme activity was optimal at pH 4.0 and its Km was 10--20 microM with sulfoiduronyl sulfoanhydromannitol. Chloride was inhibitory at high concentration and among divalent metal ions, only copper was inhibitory. Nitrocatechol sulfate was not a substrate, but did show competitive inhibition. Its Ki for iduronate sulfatase was similar to its Km for arylsulfatase, suggesting a similarity in the substrate binding sites of iduronate sulfatase and arylsulfatases.
从人肝脏中纯化艾杜糖醛酸硫酸酯酶，用于研究硫酸皮肤素的降解途径。实现了总体80倍的纯化，更重要的是，该制剂不含α-L-艾杜糖醛酸酶、β-葡萄糖醛酸酶、N-乙酰半乳糖胺4-硫酸酯硫酸酯酶（芳基硫酸酯酶B），且β-N-乙酰己糖胺酶高度富集。肝脏酶似乎由几种分子形式组成。该酶活性在pH 4.0时最佳，其对磺基艾杜糖醛酸硫代脱水甘露糖醇的Km为10 - 20μM。高浓度的氯离子具有抑制作用，在二价金属离子中，只有铜具有抑制作用。硝基邻苯二酚硫酸酯不是底物，但表现出竞争性抑制。其对艾杜糖醛酸硫酸酯酶的Ki与其对芳基硫酸酯酶的Km相似，表明艾杜糖醛酸硫酸酯酶和芳基硫酸酯酶的底物结合位点具有相似性。
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