Immunogold labelling of dystrophin in human muscle, using an antibody to the last 17 amino acids of the C-terminus.
Immunogold labelling of dystrophin in human muscle, using an antibody to the last 17 amino acids of the C-terminus.
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DOI：
10.1016/0960-8966(91)90058-z
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发表时间：
1991-01-01
期刊：
影响因子：
--
通讯作者：
Worton, R G
中科院分区：
文献类型：
--
作者：
Cullen, M J;Walsh, J;Worton, R G
免疫标记与10 nm的金探针被用来本地化肌营养不良蛋白在人骨骼肌的超微结构水平。一抗是针对含有肌营养不良蛋白C末端最后17个氨基酸的合成肽产生的。使用这种抗体，标记几乎完全局限于一个狭窄的带，包围40 nm的质膜两侧，包括膜本身。相对于质膜的金探针的位置的直方图示出了位于膜本身或膜的细胞外表面上的模式。这些结果的一种解释是肌营养不良蛋白的C-末端插入质膜中，与它紧密相关的糖蛋白一起。金探针之间的距离的直方图显示在横向和纵向截面中在约120 nm处的模式，表明肌营养不良蛋白形成邻近质膜的网格状网络。
Immunolabelling with a 10 nm gold probe was used to localize dystrophin at the ultrastructural level in human skeletal muscle. The primary antibody was raised against a synthetic peptide containing the last 17 amino acids at the C-terminus of dystrophin. Using this antibody, labelling was almost entirely confined to a narrow band enclosing 40 nm either side of the plasma membrane and including the membrane itself. Histograms of the position of the gold probe relative to the plasma membrane showed modes lying over the membrane itself or the extracellular face of the membrane. One interpretation of these results is that the C-terminus of dystrophin is inserted in the plasma membrane alongside the glycoproteins with which it is tightly associated. Histograms of the distances between gold probes displayed modes at approximately 120 nm in both transverse and longitudinal sections suggesting that dystrophin forms a lattice-like network adjacent to the plasma membrane.