Scholte H R, Luyt-Houwen I E, Dubelaar M L, Hulsmann W C
FEBS Lett. 1986 Mar 17;198(1):47-50. doi: 10.1016/0014-5793(86)81182-6.
The formation of malonyl-CoA in rat heart is catalyzed by cytosolic acetyl-CoA carboxylase. The existence of this enzyme in heart is difficult to prove by the abundant occurrence of mitochondrial propionyl-CoA carboxylase, which is also able to catalyze the carboxylation of acetyl-CoA. We used the calcium paradox as a tool to separate cytosolic components from the remaining heart, and found that acetyl-CoA carboxylase activity was preferentially released, like lactate dehydrogenase and carnitine, while propionyl-CoA carboxylase was almost fully retained. Acetyl-CoA carboxylase activity was determined after activation by citrate ion and Mg2+. The activity decreased to 64% by 48 h of fasting.
大鼠心脏中丙二酰辅酶A的形成由胞质乙酰辅酶A羧化酶催化。由于心脏中存在大量线粒体丙酰辅酶A羧化酶,而该酶也能够催化乙酰辅酶A的羧化反应,因此很难证明心脏中存在这种酶。我们利用钙反常作为一种工具,将胞质成分与心脏的其余部分分离,发现乙酰辅酶A羧化酶活性与乳酸脱氢酶和肉碱一样,优先被释放出来,而丙酰辅酶A羧化酶几乎完全保留。在经柠檬酸离子和Mg2+激活后测定乙酰辅酶A羧化酶活性。禁食48小时后,该活性降至64%。