Pinder J C, Ohanian V, Gratzer W B
FEBS Lett. 1984 Apr 24;169(2):161-4. doi: 10.1016/0014-5793(84)80310-5.
Spectrin and protein 4.1, when added to G- or F-actin, cause the formation of short filaments, as judged by the appearance of powerful nucleating activity for G-actin polymerisation. F-Actin filaments are rapidly fragmented under physiological solvent conditions. The effect of cytochalasin E on the polymerisation reaction and the extent of reduction in the critical monomer concentration of actin when spectrin and 4.1 are added suggest that these proteins form a capping system for the more slowly growing, or 'pointed' ends of actin filaments. The interaction is not affected by calcium or by 4.9, the remaining constituent of the purified red cell membrane cytoskeleton.
血影蛋白和蛋白4.1添加到G-肌动蛋白或F-肌动蛋白中时，会导致短丝的形成，这可通过G-肌动蛋白聚合的强大成核活性的出现来判断。在生理溶剂条件下，F-肌动蛋白丝会迅速断裂。细胞松弛素E对聚合反应的影响以及添加血影蛋白和4.1时肌动蛋白临界单体浓度的降低程度表明，这些蛋白质形成了一个封端系统，作用于肌动蛋白丝生长较慢的“尖”端。这种相互作用不受钙或4.9（纯化红细胞膜细胞骨架的其余成分）的影响。
