Actin binding to the cytoplasmic surface of the plasma membrane isolated from Dictyostelium discoideum.
Actin binding to the cytoplasmic surface of the plasma membrane isolated from Dictyostelium discoideum.
复制标题
肌动蛋白与从盘基网柄菌分离的质膜的细胞质表面结合。
DOI：
10.1016/s0006-291x(80)80034-9
复制
发表时间：
1980
影响因子：
3.1
通讯作者：
Bruce S. Jacobson
中科院分区：
文献类型：
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作者：
Bruce S. Jacobson
肌动蛋白从盘基网柄菌质膜的细胞质表面解离。通过使用阳离子珠的新方法分离膜，选择性地暴露细胞质表面。当纯化的肌动蛋白被添加回膜时，结合的量与肌动蛋白浓度成正比。细胞质表面的胰蛋白酶化消除了结合，而胰凝乳蛋白酶仅部分有效。与膜结合的 F-肌动蛋白远多于 G-肌动蛋白，并且这种结合不受细胞松弛素 B 抑制。结果支持肌动蛋白与暴露在质膜细胞质表面上的独特蛋白质特异性相互作用的假设。
Actin was dissociated from the cytoplasmic surface of the plasma membrane fromDictyosteliumdiscoideum. The cytoplasmic surface was selectively exposed by isolating the membrane by a new method using cationic beads. When purified actin was added back to the membrane the amount that bound was proportional to the actin concentration. Trypsinization of the cytoplasmic surface abolished binding while chymotrypsin was only partly effective. Far more F-actin bound to the membrane than G-actin and the binding was not inhibited by cytochalasin B. The results support the hypothesis that actin specifically interacts with unique proteins exposed on the cytoplasmic surface of the plasma membrane.