Purification and properties of nucleotide pyrophosphatase from rat liver plasma membranes
Purification and properties of nucleotide pyrophosphatase from rat liver plasma membranes
复制标题
大鼠肝质膜核苷酸焦磷酸酶的纯化及性质
DOI：
10.1016/0014-5793(72)80172-8
复制
发表时间：
1972
期刊：
影响因子：
3.5
通讯作者：
E. Bischoff
中科院分区：
文献类型：
--
作者：
K. Decker;E. Bischoff
当添加到分离的无血红蛋白灌注的大鼠肝脏中时，各种核苷酸遭受其焦磷酸键的快速裂解[1，21]。这种能力归因于存在于肝脏质膜中的核苷酸焦磷酸酶活性。在离体大鼠肝质膜中描述了类似的性质以及磷酸二酯酶型活性和从ATP释放焦磷酸盐[3-9]。这些不同的活动被认为是属于一个单一的酶[8，9];一个纯的酶，然而，是必要的，以证明这一点。本报告涉及的溶解和纯化的蛋白质从大鼠肝细胞质膜，催化裂解的各种核苷酸的释放相应的核苷-5 '-单磷酸的明显homogeneity。它基本上不含5 '-核苷酸酶和磷酸酶活性。该酶的底物和抑制剂特异性表明它既是核苷酸焦磷酸酶又是磷酸二酯酶。
Various nucleotides suffer a rapid cleavage of their pyrophosphate bonds when added to the isolated hemoglobin-free perfused rat liver [1, 21. This capacity was attributed to a nucleotide pyrophosphatase activity residing in the plasma membranes of the liver. Similar properties as well as a phosphodiesterase-type activity and a pyrophosphate liberation from ATP in isolated rat liver plasma membranes were described [3-9]. These different activities were supposed to belong to a single enzyme [8, 9J; a pure enzyme, however, was necessary to prove this point.This report deals with the solubilization and purification to apparent homogeneity of a protein from rat liver plasma membranes which catalyzes the cleavage of a variety of nucleotides with the liberation of the respective nucleoside-5’-monophosphates. It is essentially free of 5’-nucleotidase and phosphatase activities. The substrate and inhibitor specificity of the enzyme show it to be both a nucleotide pyrophosphatase and a phosphodiesterase.