McKean M L, Silver M J, Authi K S, Crawford N
FEBS Lett. 1986 Jan 20;195(1-2):38-42. doi: 10.1016/0014-5793(86)80125-9.
We have investigated the distribution and fatty acid preference of two acyl-CoA transferase activities in a human platelet mixed membrane fraction and in well-characterised surface and intracellular membrane subfractions prepared from it by high-voltage free-flow electrophoresis. One transferase inserts long-chain unsaturated fatty acids into 1-acyllysophosphatidylcholine (1-acyl-LPC) and the other into lyso-platelet-activating factor (LPAF). Both transferase activities were approx. 4-fold enriched in the intracellular membranes with respect to their specific activities in the mixed membranes. The surface membrane activities were correspondingly depleted. Using 1-acyl-LPC as the acceptor, all the intracellular membrane preparations showed transferase preference for the CoA ester of 8,11,14-eicosatrienoic acid. In contrast when LPAF was the acceptor the CoA esters of linoleic and arachidonic acid were the preferred donors.
我们研究了人血小板混合膜组分以及通过高压自由流电泳从该混合膜组分制备的、特性明确的表面膜和细胞内膜亚组分中两种酰基辅酶A转移酶活性的分布和脂肪酸偏好。一种转移酶将长链不饱和脂肪酸插入1-酰基溶血磷脂酰胆碱（1-酰基-LPC），另一种转移酶将长链不饱和脂肪酸插入溶血血小板激活因子（LPAF）。相对于它们在混合膜中的比活性，两种转移酶活性在细胞内膜中均约富集4倍。表面膜活性相应降低。以1-酰基-LPC作为受体时，所有细胞内膜制剂均显示转移酶对8,11,14-二十碳三烯酸的辅酶A酯具有偏好性。相比之下，当LPAF作为受体时，亚油酸和花生四烯酸的辅酶A酯是首选供体。
