Purification and partial characterization of arylsulphatase C from human placental microsomes.
Purification and partial characterization of arylsulphatase C from human placental microsomes.
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从人胎盘微粒体中纯化芳基硫酸酯酶 C 并进行部分表征。
DOI：
10.1016/0304-4165(83)90313-6
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发表时间：
1983
期刊：
影响因子：
--
通讯作者：
Gary J. Burns
中科院分区：
文献类型：
--
作者：
Gary J. Burns
Arylsulphatase C (EC 3.1.6.1) has been purified 300-fold from human placental microsomes using a four step procedure involving solubilization with Triton X-100, chromatography on hydroxyapatite, column chromatofocussing and ion-exchange chromatography on DEAE-Sepharose. The purified enzyme is electrophoretically homogeneous and has a molecular weight of 440 000 as determined by polyacrylamide gradient gel electrophoresis. On analysis of the preparation by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate a polypeptide of molecular weight 74 000 was observed, suggesting that the enzyme as purified may be a hexamer. The behaviour of the enzyme during chromatofocussing indicates the enzyme has a pIof 6.56. Steroid sulphatase, as measured by activity towards dehydroepiandrosterone sulphate, co-purifies with arylsulphatase C suggesting that both activities are due to a single enzyme.
