纯化的大鼠肾脏线粒体和胞质转脒基酶性质的比较。

Comparison of the properties of purified mitochondrial and cytosolic rat kidney transamidinase.

Tormanen C D

Department of Chemistry, Central Michigan University, Mount Pleasant.

Int J Biochem. 1990;22(11):1243-50. doi: 10.1016/0020-711x(90)90305-m.

Abstract

Mitochondrial rat kidney transamidinase was solubilized by two extractions with the surfactant Zwittergent 3-14. 2. Mitochondrial and cytosolic forms of rat kidney transamidinase were purified by chromatography on DEAE-Trisacryl M, phenyl-Sepharose Cl-4B and hydroxylapatite columns. 3. The specific activity of purified mitochondrial enzyme was significantly higher than purified cytosolic enzyme. 4. The subunit molecular mass, the electrophoretic mobility under nondenaturing conditions, and the activation energy were similar for purified mitochondrial and cytosolic transamidinase.

摘要

用表面活性剂两性离子去污剂3-14进行两次抽提，使大鼠肾线粒体转脒基酶溶解。2. 通过在DEAE-三羟甲基氨基甲烷琼脂糖M、苯基琼脂糖CL-4B和羟基磷灰石柱上进行层析，纯化大鼠肾转脒基酶的线粒体形式和胞质形式。3. 纯化的线粒体酶的比活性显著高于纯化的胞质酶。4. 纯化的线粒体和胞质转脒基酶的亚基分子量、非变性条件下的电泳迁移率和活化能相似。