来自海洋腹足纲动物红螺肝脏的两种糖硫酸酯酶。部分纯化及性质

Two glycosulfatases from the liver of a marine gastropod, Charonia lampas. Partial purification and properties.

作者信息

Hatanaka H, Ogawa Y, Egami F

出版信息

J Biochem. 1976 Jan;79(1):27-34. doi: 10.1093/oxfordjournals.jbchem.a131054.

DOI:10.1093/oxfordjournals.jbchem.a131054

Abstract

Two glycosulfatases [EC 3.1.6.3], I and II, were purified 31.3- and 33.9-fold respectively, from a crude extract of the liver of Charonia lampas. The purification was carried out by the following chromatographic procedures; phosphocellulose, Sephadex G-150, Concanavalin A-Sepharose and isoelectric focussing. The enzyme preparations obtained were practically free from arylsulfatase [EC 3.1.6.1] contamination. Both glycosulfatases are probably glycoproteins differing in their carbohydrate moieties. The molecular weights of glycosulfatase I and II were estimated to be about 112,000 and 79,000 respectively. They had the same optimum pH of 5.5, and the same Km value of 25.0 mM for glucose 6-sulfate.

摘要

从长旋螺肝脏粗提物中分别纯化出两种硫酸酯酶[EC 3.1.6.3]，即I型和II型，纯化倍数分别为31.3倍和33.9倍。纯化过程通过以下色谱步骤进行：磷酸纤维素、葡聚糖凝胶G-150、伴刀豆球蛋白A-琼脂糖凝胶和等电聚焦。所获得的酶制剂几乎没有芳基硫酸酯酶[EC 3.1.6.1]污染。两种硫酸酯酶可能都是糖蛋白，其碳水化合物部分有所不同。I型和II型硫酸酯酶的分子量估计分别约为112,000和79,000。它们具有相同的最适pH值5.5，对6-硫酸葡萄糖的Km值均为25.0 mM。