大鼠各种组织中可溶性硫胺三磷酸酶活性与非特异性磷酸酶的关系。

Penttinen H K, Uotila L

Med Biol. 1981 Jun;59(3):177-84.

Polyacrylamide gel electrophoresis was used to investigate the relation of the soluble thiamine triphosphatase activity of various rat tissues to other phosphatases. This technique separated the thiamine triphosphatase of rat brain, heart, kidney, liver, lung, muscle and spleen from alkaline phosphatase (EC 3.1.3.1), acid phosphatase (EC 3.1.3.2) and other nonspecific phosphatase activities. In contrast, the hydrolytic activity for thiamine triphosphate in rat intestine moved identically with alkaline phosphatase in gel electrophoresis. Thiamine triphosphatase from rat liver and brain was also separated from alkaline phosphatase and acid phosphatase by gel chromatography on Sephadex G-100. This gave an apparent molecular weight of about 30,000 and a Stokes radius of 2.5 nanometers for brain and liver thiamine triphosphatase. The intestinal thiamine triphosphatase activity of the rat was eluted from the Sephadex G-100 column as two separate peaks (with apparent molecular weights of over 200,000 and 123,000) which exactly corresponded to the peaks of alkaline phosphatase. The isoelectric point (pI) of the brain thiamine triphosphatase was 4.6 (4 degrees C). The partially purified thiamine triphosphatase from brain and liver was highly specific for thiamine triphosphate. The results suggest that, apart from the intestine, the rat tissues studied contain a specific enzyme, thiamine triphosphatase (EC 3.6.1.28). The specific enzyme is responsible for most of the thiamine triphosphatase activity in these tissues. Rat intestine contains a high thiamine triphosphatase activity but all of it appears to be due to alkaline phosphatase.

采用聚丙烯酰胺凝胶电泳法研究了大鼠各组织中可溶性硫胺三磷酸酶活性与其他磷酸酶之间的关系。该技术将大鼠脑、心脏、肾脏、肝脏、肺、肌肉和脾脏中的硫胺三磷酸酶与碱性磷酸酶（EC 3.1.3.1）、酸性磷酸酶（EC 3.1.3.2）及其他非特异性磷酸酶活性分离开来。相比之下，大鼠肠道中硫胺三磷酸的水解活性在凝胶电泳中与碱性磷酸酶的迁移情况相同。大鼠肝脏和脑中的硫胺三磷酸酶也通过Sephadex G - 100凝胶色谱法与碱性磷酸酶和酸性磷酸酶分离开。结果显示，脑和肝脏硫胺三磷酸酶的表观分子量约为30,000，斯托克斯半径为2.5纳米。大鼠肠道中的硫胺三磷酸酶活性从Sephadex G - 100柱上洗脱下来呈现为两个单独的峰（表观分子量分别超过200,000和123,000），这与碱性磷酸酶的峰完全对应。脑硫胺三磷酸酶的等电点（pI）为4.6（4℃）。从脑和肝脏中部分纯化得到的硫胺三磷酸酶对硫胺三磷酸具有高度特异性。结果表明，除肠道外，所研究的大鼠组织中含有一种特异性酶，即硫胺三磷酸酶（EC 3.6.1.28）。这种特异性酶负责这些组织中大部分的硫胺三磷酸酶活性。大鼠肠道含有较高的硫胺三磷酸酶活性，但所有这些活性似乎都归因于碱性磷酸酶。