Spectrin oligomers: a structural feature of the erythrocyte cytoskeleton.
Spectrin oligomers: a structural feature of the erythrocyte cytoskeleton.
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血影蛋白寡聚物：红细胞细胞骨架的结构特征。
DOI：
10.1002/jsscb.380170308
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发表时间：
1981
期刊：
影响因子：
--
通讯作者：
Marchesi,VT
中科院分区：
文献类型：
--
作者：
Morrow,JS;HaighJr,WB;Marchesi,VT
Spectrin通过浓度驱动的过程可逆地自结合到高分子量的低聚物，其缔合常数约为105mol−1。这种关联在pH值、离子强度和温度等生理条件下表现突出。它被尿素破坏，但不被Triton X‐100破坏。谱蛋白结合的过程在数学上似乎与原肌球蛋白相似，尽管其机制可能不同。与红细胞膜骨架中其他重要的蛋白关联相比，Spectrin关联较弱。这些弱关联和强关联的联系暗示了膜骨架自发组装的过程。这种涉及弱关联的亲和调节组装可能是许多膜控制机制的焦点。
Spectrin reversibly self‐associates to high molecular weight oligomers through a concentration‐driven process characterized by association constants of about 105mol−1. This association is prominent under physiological conditions of pH, ionic strength, and temperature. It is disrupted by urea, but not Triton X‐100. The process of spectrin association appears mathematically to resemble that for tropomyosin, although the mechanism is probably different. Spectrin association is weak compared to other prominent protein–protein associations in the red cell membrane skeleton. The linkage of these weak and strong associations suggests a process whereby the membrane skelton spontaneously assembles. Such affinity‐modulated assembly involving weak associations is likely to be the focus of numerous membrane control mechanisms.