Ultrastructure of the intact skeleton of the human erythrocyte membrane.
Ultrastructure of the intact skeleton of the human erythrocyte membrane.
复制标题
人红细胞膜完整骨骼的超微结构。
DOI：
10.1083/jcb.102.3.997
复制
发表时间：
1986-03
影响因子：
7.8
通讯作者：
STECK, TL
中科院分区：
文献类型：
--
作者：
SHEN, BW;JOSEPHS, R;STECK, TL
在 Triton X-100 中从分离的人红细胞膜中分离出丝状骨架，铺展在有孔碳膜上，进行负染色，并在透射电子显微镜中观察到完整且未固定的情况。检查了两种形式的骨架：(a) 基本骨架，用 1.5 M NaCl 剥离辅助蛋白，使其主要含有多肽带 1、2、4.1 和 5； (b) 未剥离的骨骼，其中还含有锚蛋白和带 3 等辅助蛋白以及残留脂质的小斑块。刚准备好的骷髅高度凝结。在低离子强度和二硫苏糖醇存在下孵育一个小时或更长时间会导致骨架膨胀，从而大大增加其元素的可见度。扩张可能反映了血影蛋白从紧凑结构向细长结构的打开。扩展的骨架似乎被组织为由多个（5-8）血影蛋白四聚体连接的短肌动蛋白丝网络。在未剥离的制剂中，在血影蛋白丝的中心附近观察到球状物质，可能对应于锚蛋白与带3寡聚体的复合物。其中一些小球连接着成对的血影蛋白丝。用最少的扰动制备的骨骼具有增厚的肌动蛋白原丝，这可能反映了辅助蛋白的存在。这些肌动蛋白丝的长度高度均匀，平均为 33 +/- 5 nm。这是非肌肉原肌球蛋白的长度。由于存在几乎足够的原肌球蛋白来饱和 F-肌动蛋白，因此我们的数据支持原肌球蛋白可能决定红细胞膜中肌动蛋白原丝的长度的假设。
Filamentous skeletons were liberated from isolated human erythrocyte membranes in Triton X-100, spread on fenestrated carbon films, negatively stained, and viewed intact and unfixed in the transmission electron microscope. Two forms of the skeleton were examined: (a) basic skeletons, stripped of accessory proteins with 1.5 M NaCl so that they contain predominantly polypeptide bands 1, 2, 4.1, and 5; and (b) unstripped skeletons, which also bore accessory proteins such as ankyrin and band 3 and small plaques of residual lipid. Freshly prepared skeletons were highly condensed. Incubation at low ionic strength and in the presence of dithiothreitol for an hour or more caused an expansion of the skeletons, which greatly increased the visibility of their elements. The expansion may reflect the opening of spectrin from a compact to an elongated disposition. Expanded skeletons appeared to be organized as networks of short actin filaments joined by multiple (5-8) spectrin tetramers. In unstripped preparations, globular masses were observed near the centers of the spectrin filaments, probably corresponding to complexes of ankyrin with band 3 oligomers. Some of these globules linked pairs of spectrin filaments. Skeletons prepared with a minimum of perturbation had thickened actin protofilaments, presumably reflecting the presence of accessory proteins. The length of these actin filaments was highly uniform, averaging 33 +/- 5 nm. This is the length of nonmuscle tropomyosin. Since there is almost enough tropomyosin present to saturate the F- actin, our data support the hypothesis that tropomyosin may determine the length of actin protofilaments in the red cell membrane.
登录
查看更多内容
影响因子：
64.5
作者：
COHEN, CM;TYLER, JM;BRANTON, D
通讯作者：
BRANTON, D
影响因子：
64.8
作者：
EGELMAN, EH;FRANCIS, N;DEROSIER, DJ
通讯作者：
DEROSIER, DJ
DOI：
10.1002/jss.400060303
发表时间：
1977-01-01
期刊：
JOURNAL OF SUPRAMOLECULAR STRUCTURE
影响因子：
--
作者：
HAINFELD, JF;STECK, TL
通讯作者：
STECK, TL
影响因子：
64.8
作者：
LIU, SC;PALEK, J
通讯作者：
PALEK, J
影响因子：
7.8
作者：
JOHNSON, RM;TAYLOR, G;MEYER, DB
通讯作者：
MEYER, DB