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哺乳动物脑2'-核苷酸酶的纯化及性质

Purification and properties of 2'-nucleotidase from mammalian brain.

作者信息

Nakamura S, Yamao S, Ito J, Kameyama M

出版信息

Biochim Biophys Acta. 1979 May 10;568(1):30-8. doi: 10.1016/0005-2744(79)90270-5.

Abstract

A nucleotidase specific for 2'-nucleotides was localized in both the soluble and the synaptosomal fractions of rat brain. The enzyme was partially purified from the soluble fraction of bovine brain. The s20,w was 4.9 S with an estimated molecular weight of about 70 000. The optimum pH was 8.0 and Km value for 2'-AMP was 5.5 . 10(-4) M. The substrate and inhibitor specificities of the enzyme were examined. The nucleotidase has an absolute requirement for Mg2+ but neither Fe3+ nor Ca2+ acted as replacement ions. In fact, Mn2+ and Ca2+ inhibited the Mg2+-dependent 2'-nucleotidase.

摘要

一种对2'-核苷酸具有特异性的核苷酸酶定位于大鼠脑的可溶性部分和突触体部分。该酶从牛脑的可溶性部分进行了部分纯化。沉降系数s20,w为4.9 S,估计分子量约为70000。最适pH为8.0,2'-AMP的Km值为5.5×10⁻⁴ M。对该酶的底物和抑制剂特异性进行了检测。该核苷酸酶对Mg²⁺有绝对需求,而Fe³⁺和Ca²⁺都不能作为替代离子。实际上,Mn²⁺和Ca²⁺会抑制依赖Mg²⁺的2'-核苷酸酶。

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