Bisaccia F, Indiveri C, Palmieri F
Biochim Biophys Acta. 1985 Dec 16;810(3):362-9. doi: 10.1016/0005-2728(85)90222-1.
The alpha-oxoglutarate carrier from pig heart mitochondria has been solubilized with Triton X-114 and purified by chromatography on hydroxyapatite and celite in the presence of cardiolipin. When applied to SDS gel electrophoresis, the purified protein consists of only a single protein band with an apparent Mr of 31.5 kDa. It corresponds to band 4 of the five protein bands previously identified in the hydroxyapatite pass-through of Triton X-114 solubilized heart mitochondria (Bisaccia, F. and Palmieri, F. (1984) Biochim. Biophys. Acta 766, 386-394). When reconstituted into liposomes the alpha-oxoglutarate transport protein catalyzes a phthalonate-sensitive alpha-oxoglutarate/alpha-oxoglutarate exchange. It is purified 250-fold with a recovery of 62% and a protein yield of 0.1% with respect to the mitochondrial extract. The properties of the reconstituted carrier, i.e., the requirements for a counteranion, the substrate specificity and the inhibitor sensitivity, are similar to those described for alpha-oxoglutarate transport in mitochondria.
猪心线粒体中的α-酮戊二酸载体已用Triton X-114增溶，并在心磷脂存在下通过羟基磷灰石和硅藻土色谱法纯化。当应用于SDS凝胶电泳时，纯化后的蛋白质仅由一条单一的蛋白带组成，其表观分子量为31.5 kDa。它对应于先前在Triton X-114增溶的心脏线粒体的羟基磷灰石穿透物中鉴定出的五条蛋白带中的第4条带（Bisaccia, F.和Palmieri, F. (1984) Biochim. Biophys. Acta 766, 386 - 394）。当重新组装到脂质体中时，α-酮戊二酸转运蛋白催化邻苯二甲酸盐敏感的α-酮戊二酸/α-酮戊二酸交换。相对于线粒体提取物，其纯化了250倍，回收率为62%，蛋白质产量为0.1%。重新组装的载体的特性，即对抗衡阴离子的要求、底物特异性和抑制剂敏感性，与线粒体中α-酮戊二酸转运所描述的特性相似。
