Department of Bacteriology and Biochemistry, University of Idaho, Moscow, Idaho 83843.
Plant Physiol. 1992 Dec;100(4):2030-4. doi: 10.1104/pp.100.4.2030.
The tricarboxylate transporter was solubilized from pea (Pisum sativum) mitochondria with Triton X-114, partially purified over a hydroxylapatite column, and reconstituted in phospholipid vesicles. The proteoliposomes exchanged external [(14)C]citrate for internal citrate or malate but not for preloaded d,l-isocitrate. Similarly, although external malate, succinate, and citrate competed with [(14)C]citrate in the exchange reaction, d,l-isocitrate and phosphoenolpyruvate did not. This tricarboxylate transporter differed from the equivalent activity from animal tissues in that it did not transport isocitrate and phosphoenolpyruvate. In addition, tricarboxylate transport in isolated plant mitochondria, as well as that measured with the partially purified and reconstituted transporter, was less active than the transporter isolated from animal tissues.
三羧酸载体蛋白用 Triton X-114 从豌豆（Pisum sativum）线粒体中溶解出来，经羟磷灰石柱部分纯化，并在磷脂囊泡中再构成。这些蛋白囊泡可以交换外部的[(14)C]柠檬酸与内部的柠檬酸或苹果酸，但不能交换预先加载的 d,l-异柠檬酸。同样，尽管外部的苹果酸、琥珀酸和柠檬酸在交换反应中与[(14)C]柠檬酸竞争，但 d,l-异柠檬酸和磷酸烯醇丙酮酸却不竞争。这种三羧酸载体蛋白与来自动物组织的等效活性不同，因为它不运输异柠檬酸和磷酸烯醇丙酮酸。此外，与从动物组织中分离的载体相比，分离的植物线粒体中的三羧酸转运以及用部分纯化和再构成的载体测量的三羧酸转运活性较低。
