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牛肝溶酶体腺苷5'-磷酸硫酸水解酶的纯化及性质。一种具有焦磷酸酶和磷酸二酯酶活性的非特异性酶。

Purification and properties of bovine liver lysosomal adenosine 5'-phosphosulphate sulphohydrolase. A non-specific enzyme with pyrophosphatase and phosphodiesterase activities.

作者信息

Rogers K M, White G F, Dodgson K S

出版信息

Biochim Biophys Acta. 1978 Nov 10;527(1):70-85. doi: 10.1016/0005-2744(78)90257-7.

Abstract

Bovine liver lysosomal adenosine 5'-phosphosulphate sulphohydrolase (EC 3.6.2.1) was purified to apparent homogeneity. The molecular weight of the enzyme was 53 000 by sodium dodecyl sulphate polyacrylamide gel electrophoresis and 56 000 by BioGel P-150 gel filtration. The substrate specificity of the enzyme was studied. The several substrates towards which the enzyme preparation showed high activity were used to establish that a single enzyme was responsible for the different activities. This multiple specificity provides a possible explanation of the physiological role of lysosomal adenosine 5'-phosphosulphate sulphohydrolase.

摘要

牛肝溶酶体腺苷5'-磷酸硫酸水解酶(EC 3.6.2.1)被纯化至表观均一。通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳测定该酶的分子量为53000,通过BioGel P - 150凝胶过滤测定为56000。研究了该酶的底物特异性。使用该酶制剂表现出高活性的几种底物来确定单一酶负责不同的活性。这种多重特异性为溶酶体腺苷5'-磷酸硫酸水解酶的生理作用提供了一种可能的解释。

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