Lund H, Woldegiorgis G
Biochim Biophys Acta. 1986 Sep 12;878(2):243-9. doi: 10.1016/0005-2760(86)90152-9.
Carnitine palmitoyltransferase activity and malonyl-CoA binding capacity have been studied in Triton X-100 extracts and membrane residues of rat liver mitochondria. Rat liver mitochondria extracted twice with 0.5% Triton X-100 in a salt-free medium showed increased specific binding of [2-14C]malonyl-CoA when compared with intact mitochondria. High malonyl-CoA binding required the presence of salts and was inhibited by albumin. Further solubilization of the membrane residues in the Triton/KCl medium and subsequent hydroxylapatite chromatography gave a complete separation of carnitine palmitoyltransferase and malonyl-CoA binding. The results show that malonyl-CoA binds to mitochondrial component(s) which is different from and more difficult to extract from the mitochondrial membrane than most of the carnitine palmitoyltransferase.
已对大鼠肝脏线粒体的Triton X-100提取物和膜残留物中的肉碱棕榈酰转移酶活性及丙二酰辅酶A结合能力进行了研究。在无盐培养基中用0.5% Triton X-100提取两次的大鼠肝脏线粒体，与完整线粒体相比，显示出[2-14C]丙二酰辅酶A的特异性结合增加。高丙二酰辅酶A结合需要盐的存在，并受到白蛋白的抑制。在Triton/KCl培养基中对膜残留物进行进一步增溶，随后进行羟基磷灰石层析，可将肉碱棕榈酰转移酶和丙二酰辅酶A结合完全分离。结果表明，丙二酰辅酶A与线粒体成分结合，该成分不同于大多数肉碱棕榈酰转移酶，且比其更难从线粒体膜中提取。
