Sheetz M P
J Cell Biol. 1979 Apr;81(1):266-70. doi: 10.1083/jcb.81.1.266.
The human erythrocyte contains a complex of peripheral membrane proteins which forms an extensive network or cytoskeleton on the cytoplasmic membrane surface. When I treat erythrocyte cytoskeletons with deoxyribonuclease I (DNase I), the cytoskeletons dissociate and erythrocyte actin is solubilized. The dissociation of the cytoskeletons by DNase I parallels the disruption of actin filaments in vitro by DNase I and is blocked by the addition of action to the DNase I. Large protein complexes remain after DNase I disrupts the cytoskeletons, but these complexes are no longer visible in the light microscope nor sedimentable and are selectively depleted with respect to actin. From these studies, I suggest that DNase I binds to and solubilizes actin, which serves as a structural link between protein complexes in the erythrocyte cytoskeleton.
人类红细胞含有一组外周膜蛋白复合物，该复合物在细胞质膜表面形成一个广泛的网络或细胞骨架。当我用脱氧核糖核酸酶I（DNase I）处理红细胞细胞骨架时，细胞骨架会解离，红细胞肌动蛋白会溶解。DNase I使细胞骨架解离的过程与体外DNase I破坏肌动蛋白丝的过程相似，并且通过向DNase I中添加肌动蛋白可以阻止这种解离。DNase I破坏细胞骨架后会留下大的蛋白质复合物，但这些复合物在光学显微镜下不再可见，也不可沉降，并且相对于肌动蛋白有选择性地减少。从这些研究中，我认为DNase I结合并溶解肌动蛋白，肌动蛋白作为红细胞细胞骨架中蛋白质复合物之间的结构连接。
