Sliwkowski M X, Hartmanis M G
Anal Biochem. 1984 Sep;141(2):344-7. doi: 10.1016/0003-2697(84)90052-6.
Thiolase and NADP-dependent 3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri were purified by ion-exchange chromatography to near homogeneity in a simultaneous, single-step procedure. The yield of both enzymes was greater than 80%. Thiolase was purified approximately 8-fold with sp act 115 units/mg, whereas 3-hydroxybutyryl-CoA dehydrogenase was purified 14-fold with sp act 292 units/mg. Isoelectric points of the enzymes are 7.7 for thiolase and 7.8 for 3-hydroxybutyryl-CoA dehydrogenase. Milligram quantities of each of these enzymes are readily obtained from this fatty acid-producing organism.
来自克氏梭菌的硫解酶和NADP依赖性3-羟基丁酰辅酶A脱氢酶通过离子交换色谱法在一个同步的单步程序中被纯化至接近均一状态。两种酶的产量均大于80%。硫解酶纯化了约8倍，比活性为115单位/毫克，而3-羟基丁酰辅酶A脱氢酶纯化了14倍，比活性为292单位/毫克。硫解酶的等电点为7.7，3-羟基丁酰辅酶A脱氢酶的等电点为7.8。从这种产生脂肪酸的生物体中很容易获得毫克量的每种酶。
