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关于泛醌在磷脂酰胆碱双分子层中的定位

On the localization of ubiquinone in phosphatidylcholine bilayers.

作者信息

Stidham M A, McIntosh T J, Siedow J N

出版信息

Biochim Biophys Acta. 1984 Dec 18;767(3):423-31. doi: 10.1016/0005-2728(84)90040-9.

Abstract

The location of ubiquinone-10 in phospholipid bilayers was analyzed using a variety of physical techniques. Specifically, we examined the hypothesis that ubiquinone localizes at the geometric center of phospholipid bilayers. Light microscopy of dipalmitoylphosphatidylcholine at room temperature in the presence of 0.05-0.5 mol fraction ubiquinone showed two separate phases, one birefringent lamellar phase and one phase that consisted of isotropic liquid droplets. The isotropic phase had a distinct yellow color, characteristic of melted ubiquinone. [13C]NMR spectroscopy of phosphatidylcholine liposomes containing added ubiquinone indicated a marked effect on the 13C-spin lattice relaxation times of the lipid hydrocarbon chain atoms near the polar head region of the bilayer, but almost no effect on those atoms nearest the center of the bilayer. X-ray diffraction experiments showed that for phosphatidylcholine bilayers, both in the gel and liquid-crystal-line phases, the presence of ubiquinone did not change either the lamellar repeat period or the wide-angle reflections from the lipid hydrocarbon chains. In electron micrographs, the hydrophobic freeze-fracture surfaces of bilayers in the rippled (P beta') phase were also unmodified by the presence of ubiquinone. These results indicate that the ubiquinone which does partition into the bilayer is not localized preferentially between the monolayers, and that an appreciable fraction of the ubiquinone forms a separate phase located outside the lipid bilayer.

摘要

运用多种物理技术分析了辅酶Q-10在磷脂双分子层中的位置。具体而言,我们检验了辅酶Q定位于磷脂双分子层几何中心的假说。在0.05 - 0.5摩尔分数辅酶Q存在的情况下,对室温下的二棕榈酰磷脂酰胆碱进行光学显微镜观察,发现有两个分离的相,一个是双折射层状相,另一个是由各向同性液滴组成的相。各向同性相具有明显的黄色,这是熔化的辅酶Q的特征颜色。对添加了辅酶Q的磷脂酰胆碱脂质体进行的[13C]核磁共振光谱分析表明,其对双分子层极性头部区域附近脂烃链原子的13C自旋晶格弛豫时间有显著影响,但对最靠近双分子层中心的那些原子几乎没有影响。X射线衍射实验表明,对于磷脂酰胆碱双分子层,无论是在凝胶相还是液晶相,辅酶Q的存在既没有改变层状重复周期,也没有改变来自脂烃链的广角反射。在电子显微镜照片中,起伏(Pβ')相双分子层的疏水冷冻断裂表面也未因辅酶Q的存在而改变。这些结果表明,确实分配到双分子层中的辅酶Q并非优先定位于单分子层之间,并且相当一部分辅酶Q形成了位于脂质双分子层外部的一个单独相。

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