如果用外膜丙二酰辅酶A结合蛋白进行重组，来自肝线粒体内膜的肉碱棕榈酰转移酶（CPT2）会被丙二酰辅酶A抑制。
Carnitine palmitoyltransferase (CPT2) from liver mitochondrial inner membrane becomes inhibitable by malonyl-CoA if reconstituted with outer membrane malonyl-CoA binding protein.
作者信息
Ghadiminejad I, Saggerson E D
机构信息
Department of Biochemistry, University College London, UK.
出版信息
FEBS Lett. 1990 Sep 3;269(2):406-8. doi: 10.1016/0014-5793(90)81204-2.
PMID:2401367
Abstract
A soluble extract was obtained on treatment of rat liver mitochondrial outer membranes with cholate which bound [14C]malonyl-CoA but was essentially free of carnitine palmitoyltransferase (CPT) activity. Extraction of mitochondrial inner membranes with cholate readily solubilized a CPT activity which was insensitive to malonyl-CoA. Combination of these two extracts caused the CPT derived from inner membranes to become inhibitable by malonyl-CoA.
摘要
用胆酸盐处理大鼠肝脏线粒体外膜可获得一种可溶性提取物，该提取物能结合[14C]丙二酰辅酶A，但基本没有肉碱棕榈酰转移酶（CPT）活性。用胆酸盐提取线粒体内膜能轻易溶解一种对丙二酰辅酶A不敏感的CPT活性。将这两种提取物混合会使源自内膜的CPT变得可被丙二酰辅酶A抑制。
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Carnitine palmitoyltransferase (CPT2) from liver mitochondrial inner membrane becomes inhibitable by malonyl-CoA if reconstituted with outer membrane malonyl-CoA binding protein.如果用外膜丙二酰辅酶A结合蛋白进行重组，来自肝线粒体内膜的肉碱棕榈酰转移酶（CPT2）会被丙二酰辅酶A抑制。
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