Rigobello M P, Donella-Deana A, Cesaro L, Bindoli A
Dipartimento di Chimica Biologica, Università di Padova, Viale G. Colombo 3, 35121 Padova, Italy.
Biochem J. 2001 Jun 1;356(Pt 2):567-70. doi: 10.1042/0264-6021:3560567.
Here we report the localization of protein disulphide isomerase (PDI) in the mitochondrial compartments, comparing it with that of thioredoxin reductase. The latter enzyme is present mostly in the matrix, whereas PDI is located at the level of the outer membrane. We characterize the different submitochondrial fractions with specific marker enzymes. PDI, whether isolated from whole mitochondria or from purified outer membranes, exhibits the same electrophoretic mobility, indicating identical molecular masses. Moreover, immunoblot analysis with monoclonal anti-PDI antibody shows immunoreactivity only with the microsomal PDI, indicating the specificity of the mitochondrial isoform. The significance of these findings is discussed with reference to the potential role of PDI and thioredoxin reductase in regulating the mitochondrial functions dependent on the thiol-disulphide transition.
在此，我们报告了蛋白质二硫键异构酶（PDI）在线粒体区室中的定位，并将其与硫氧还蛋白还原酶的定位进行了比较。后一种酶主要存在于线粒体基质中，而PDI则位于外膜水平。我们用特定的标记酶对不同的亚线粒体组分进行了表征。PDI无论是从完整的线粒体中分离出来还是从纯化的外膜中分离出来，都表现出相同的电泳迁移率，表明其分子量相同。此外，用单克隆抗PDI抗体进行的免疫印迹分析显示，仅与微粒体PDI有免疫反应性，这表明线粒体异构体具有特异性。我们结合PDI和硫氧还蛋白还原酶在调节依赖硫醇-二硫键转变的线粒体功能中的潜在作用，讨论了这些发现的意义。
