Emyanitoff R G, Kelly P J
J Gen Microbiol. 1982 Aug;128(8):1767-71. doi: 10.1099/00221287-128-8-1767.
Malate dehydrogenase (MDH; EC 1.1.1.37) from Dictyostelium discoideum was purified and characterized MDH activity from whole cells was purified 275-fold. The mitochondrial and cytoplasmic MDH present co-purified through three ion exchange and affinity chromatography steps. The isoenzymes were barely separable by either disc gel electrophoresis or isoelectric focusing. The purified preparation containing both isoenzymes had a single pH optimum (9.3-9.5) and an apparent molecular weight of 70000. It exhibited linear kinetics and responded to known inhibitors of MDH, i.e. thyroxine and hydroxymalonate. Michaelis and dissociation constants obtained with this preparation were similar to those obtained with a 10-fold purified mitochondrial MDH.
对盘基网柄菌的苹果酸脱氢酶（MDH；EC 1.1.1.37）进行了纯化和特性分析。全细胞中的MDH活性被纯化了275倍。线粒体和细胞质中的MDH通过三步离子交换和亲和层析共纯化。这两种同工酶通过圆盘凝胶电泳或等电聚焦几乎无法分离。含有这两种同工酶的纯化制剂有一个单一的最适pH值（9.3 - 9.5），表观分子量为70000。它呈现出线性动力学，并且对已知的MDH抑制剂，即甲状腺素和羟基丙二酸有反应。用该制剂获得的米氏常数和解离常数与用纯化10倍的线粒体MDH获得的常数相似。
