Huth W, Alves F
Biochim Biophys Acta. 1985 Aug 23;830(3):274-81. doi: 10.1016/0167-4838(85)90283-3.
The mitochondrial acetyl-CoA acetyltransferase (acetyl-CoA:acetyl-CoA C-acetyltransferase, EC 2.3.1.9), which is involved in the biosynthesis or degradation of ketone bodies, was directly demonstrated in organ extracts applying a two-step chromatography-immunoelectrophoresis method. In liver, the enzyme can be shown in at least three forms: in an unmodified state, designated as AAT, and in the CoASH-modified forms A1 and A2, in amounts of 51.5 +/- 5.0%, 39.4 +/- 4.8% and 9.1 +/- 2.7% (areas of immunoprecipitation), respectively. This pattern, which could not be altered by a treatment with glutathione, resembles that of mitochondrial acetyl-CoA acetyltransferase in extrahepatic tissues. However, the proportion of the unmodified enzyme (AAT) is lower as compared to those in other tissues such as brain (81.5 +/- 4.4%). CoASH-modification and transformation into modified forms, which equal naturally occurring forms, can be demonstrated in vitro with acetyl-CoA acetyltransferase from both liver and brain. Thus CoASH-modification of mitochondrial acetyl-CoA acetyltransferase seems to be a process of general importance.
参与酮体生物合成或降解的线粒体乙酰辅酶A乙酰转移酶（乙酰辅酶A：乙酰辅酶A C - 乙酰转移酶，EC 2.3.1.9），采用两步色谱 - 免疫电泳法在器官提取物中得到直接证实。在肝脏中，该酶至少以三种形式存在：未修饰状态，称为AAT；以及辅酶A（CoASH）修饰形式A1和A2，其含量分别为51.5±5.0%、39.4±4.8%和9.1±2.7%（免疫沉淀面积）。这种模式不受谷胱甘肽处理的影响，类似于肝外组织中线粒体乙酰辅酶A乙酰转移酶的模式。然而，与其他组织如脑（81.5±4.4%）相比，未修饰酶（AAT）的比例较低。来自肝脏和脑的乙酰辅酶A乙酰转移酶在体外均可证明CoASH修饰并转化为与天然存在形式相同的修饰形式。因此，线粒体乙酰辅酶A乙酰转移酶的CoASH修饰似乎是一个具有普遍重要性的过程。
