Deamer D W, Boatman D E
J Cell Biol. 1980 Feb;84(2):461-7. doi: 10.1083/jcb.84.2.461.
Acyltransferase activity is present in a variety of membranes species, including liver microsomes. The substrates of this enzyme are lysophosphatides and acyl CoA derivatives. We have found that the detergent effect of these substrates can be used to solubilize rat liver microsomes. If the solubilized fraction in incubated, the acyltransferase acylates the lysophosphatide and thereby degrades the detergent effect so that vesicular membranes re-form. Gel electrophoresis patterns show that the reconstituted membranes contain all of the major protein components of the original microsomes. A marker enzyme for liver microsomes, NADPH-cytochrome c reductase, was present in the reconstituted membranes at 70% of the specific activity in the original microsomes, and freeze-fracture electron microscopy showed intramembrane particles on all fracture faces. The system may provide a useful model for studies particles on all fracture faces. This system may provide a useful model for studies of certain membrane biogenesis reactions that utilize acyltransferase in vivo.
酰基转移酶活性存在于多种膜结构中，包括肝微粒体。该酶的底物是溶血磷脂和酰基辅酶A衍生物。我们发现这些底物的去污剂作用可用于溶解大鼠肝微粒体。如果将溶解后的部分进行孵育，酰基转移酶会使溶血磷脂酰化，从而降低去污剂作用，使泡状膜重新形成。凝胶电泳图谱显示，重构膜包含原始微粒体的所有主要蛋白质成分。肝微粒体的一种标记酶——NADPH - 细胞色素c还原酶，在重构膜中的比活性为原始微粒体的70%，冷冻蚀刻电子显微镜显示所有断裂面上都有膜内颗粒。该系统可能为研究所有断裂面上的颗粒提供一个有用的模型。这个系统可能为研究体内利用酰基转移酶的某些膜生物合成反应提供一个有用的模型。
