Janski A M, Cornell N W
Biosci Rep. 1982 Feb;2(2):117-22. doi: 10.1007/BF01116178.
To study the binding to mitochondria and the phosphorylation of ATP-citrate lyase (EC 4.1.3.8), isolated rat hepatocytes were fractionated by exposure to digitonin. After incubation of hepatocytes with the hypolipidemic agent 5-(tetradecyloxy)-2-furoic acid, which decreases the cellular CoA, the amount of bound ATP-citrate lyase was increased, but the content of acid-stable phosphate in the enzyme was diminished. Glucagon, in contrast, decreased the amount of bound enzyme but increased phosphorylation. This inverse relationship might indicate either that the bound ATP-citrate lyase is less readily phosphorylated or that the phosphorylated enzyme binds less readily to mitochondria.
为研究ATP-柠檬酸裂解酶（EC 4.1.3.8）与线粒体的结合及磷酸化作用，将分离的大鼠肝细胞用洋地黄皂苷处理进行分级分离。在用降血脂剂5-（十四烷氧基）-2-糠酸孵育肝细胞后，细胞内辅酶A减少，ATP-柠檬酸裂解酶的结合量增加，但该酶中酸稳定磷酸盐的含量减少。相反，胰高血糖素降低了结合酶的量，但增加了磷酸化作用。这种相反的关系可能表明，结合的ATP-柠檬酸裂解酶不易被磷酸化，或者磷酸化的酶与线粒体的结合不太容易。
