猪子宫内膜芳基硫酸酯酶A的分离与鉴定
Isolation and characterization of the pig endometrial arylsulphatase A.
作者信息
Rahi H, Srivastava P N
出版信息
Biochem J. 1983 Jun 1;211(3):649-59. doi: 10.1042/bj2110649.
The pig endometrial arylsulphatase A was purified 3322-fold to a specific activity of 150 mumol/min per mg. The purification involved (NH4)2SO4 fractionation, chromatography on concanavalin A-Sepharose and DEAE-Sepharose, gel filtrations on Sephadex G-200 at pH 7.4 and 5, and a new preparative gel-electrophoresis technique. The homogeneous enzyme is a glycoprotein containing 20% carbohydrate. The purified enzyme has Mr about 120 000 and it contains subunits of Mr 63 000. The pig endometrial arylsulphatase A shows many properties in common with those of arylsulphatases A purified from other sources. The similarities include their low isoelectric points, the anomalous time-activity relationships, multi-pH optima, inhibition by SO3(2-), SO4(2-), phosphate ions, metal ions and nucleoside phosphates, pH- and ionic-strength-dependent polymerization and amino acid composition.
猪子宫内膜芳基硫酸酯酶A被纯化了3322倍，比活性达到每毫克150微摩尔/分钟。纯化过程包括硫酸铵分级沉淀、伴刀豆球蛋白A - 琼脂糖和二乙氨基乙基 - 琼脂糖柱层析、在pH 7.4和5条件下用葡聚糖凝胶G - 200进行凝胶过滤，以及一种新的制备性凝胶电泳技术。该纯酶是一种糖蛋白，含糖量为20%。纯化后的酶分子量约为120000，由分子量为63000的亚基组成。猪子宫内膜芳基硫酸酯酶A与从其他来源纯化的芳基硫酸酯酶A具有许多共同特性。这些相似之处包括它们的低等电点、异常的时间 - 活性关系、多pH值最佳活性、被亚硫酸根离子、硫酸根离子、磷酸根离子、金属离子和核苷磷酸抑制、pH值和离子强度依赖性聚合以及氨基酸组成。
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