Linn T C, Srere P A
J Biol Chem. 1984 Nov 10;259(21):13379-84.
Purified rat liver ATP citrate lyase is shown to bind to the microsomal fraction of rat liver. Under the same conditions the enzyme does not bind significantly to the mitochondrial fraction or to the outer membrane prepared from the mitochondrial fraction. The binding component of the microsomal fraction is further identified as the endoplasmic reticulum, and a protein component of the membrane is involved in binding. Binding decreases with increasing salt concentration. It requires more than 50 mM potassium phosphate or 60 mM potassium chloride to decrease binding significantly whereas complete inhibition of binding is observed in the presence of 0.01 mM CoA. The binding capacity of the microsomal fraction is shown to be high enough to allow most, if not all, the ATP citrate lyase present in rat liver to be bound to the microsomal fraction even when the enzyme has been induced over 10-fold by dietary manipulations. No significant difference has been found when comparing the binding of the phospho and dephospho forms of ATP citrate lyase.
纯化的大鼠肝脏ATP柠檬酸裂解酶被证明能与大鼠肝脏的微粒体部分结合。在相同条件下，该酶与线粒体部分或从线粒体部分制备的外膜没有明显结合。微粒体部分的结合成分进一步被鉴定为内质网，并且膜的一种蛋白质成分参与结合。结合随着盐浓度的增加而降低。需要超过50 mM的磷酸钾或60 mM的氯化钾才能显著降低结合，而在存在0.01 mM辅酶A的情况下观察到结合完全被抑制。即使通过饮食操作使该酶诱导超过10倍，微粒体部分的结合能力也足以使大鼠肝脏中存在的大部分（如果不是全部）ATP柠檬酸裂解酶结合到微粒体部分。比较ATP柠檬酸裂解酶的磷酸化形式和去磷酸化形式的结合时，未发现显著差异。
