VISUALIZATION OF THE PROTEIN ASSOCIATIONS IN THE ERYTHROCYTE-MEMBRANE SKELETON
VISUALIZATION OF THE PROTEIN ASSOCIATIONS IN THE ERYTHROCYTE-MEMBRANE SKELETON
复制标题
DOI：
10.1073/pnas.82.18.6153
复制
发表时间：
1985-01-01
影响因子：
11.1
通讯作者：
BRANTON, D
中科院分区：
文献类型：
--
作者：
BYERS, TJ;BRANTON, D
我们已经从直接来自完整细胞的负染色制备物中获得了[人]红细胞膜骨架的清晰图像，但其中血影蛋白网络被人工分散以允许仔细检查。我们的程序需要不到2分钟在5.degree。C在磷酸盐缓冲液中。我们发现200纳米长的血影蛋白四聚体交联的连接复合物。每个连接包含一个规则的37纳米杆，可能是一个肌动蛋白寡聚体约13个单体。密度出现在可变的地方，在网络，但不同的小球发生频率很高78 nm的血影蛋白四聚体的交界处插入端，非常接近锚蛋白的已知结合位点。最常见的是，五个或六个血影蛋白四聚体插入到每个连接处，产生一个显示出非常规则的长程有序的网络。
We have obtained clear images of the [human] erythrocyte membrane skeleton from negatively stained preparations that originate directly from the intact cell but in which the spectrin meshwork is artificially spread to allow close inspection. Our procedure requires less than 2 min at 5.degree. C in phosphate buffers. We find 200-nm-long spectrin tetramers crosslinked by junctional complexes. Each junction contains a regular 37-nm rod, probably an actin oligomer of approximately 13 monomers. Densities appear at variable places in the meshwork but distinct globules occur with great frequency 78 nm from the spectrin tetramer''s junctional insertion end, very close to the known binding site for ankyrin. Most frequently, five or six spectrin tetramers insert into each junction, producing a meshwork that displays remarkably regular long range order.