Isolation of an abundant 50,000-dalton actin filament bundling protein from Dictyostelium amoebae.
Isolation of an abundant 50,000-dalton actin filament bundling protein from Dictyostelium amoebae.
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DOI：
10.1016/s0021-9258(19)39973-9
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发表时间：
1990-02
期刊：
影响因子：
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通讯作者：
M. Demma;V. Warren;R. Hock;S. Dharmawardhane;J. Condeelis
中科院分区：
文献类型：
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作者：
M. Demma;V. Warren;R. Hock;S. Dharmawardhane;J. Condeelis
天然分子量约为 50,000 的单体肌动蛋白捆绑蛋白 (ABP-50) 已从盘基网柄菌变形虫中分离出来。 ABP-50 交联 F-肌动蛋白形成紧密堆积的束，其中一些是高度有序的。它的 Kd 为 2.1 microM，与肌动蛋白的摩尔比为 1:1。生理浓度的钙和 ATP 对这些活性没有影响。 ABP-50 在免疫学上与 30-kDa 蛋白无关，30-kDa 蛋白是先前描述的来自盘基网柄菌属的捆绑蛋白。亲和纯化的多克隆抗体的免疫荧光表明 ABP-50 位于含有肌动蛋白束的变形虫细胞皮层区域。在体内，ABP-50 与肌动蛋白的摩尔比约为 1:5。因此，ABP-50 的丰度表明它可能是这些细胞中大部分捆绑活动的原因。
A monomeric actin bundling protein with a native molecular weight of approximately 50,000 (ABP-50) has been isolated from amoebae of Dictyostelium discoideum. ABP-50 cross-links F-actin to form tightly packed bundles, some of which are highly ordered. It exhibits a Kd of 2.1 microM and a molar ratio to actin of 1:1 in bundles. Calcium and ATP at physiological concentrations have no effect on these activities. ABP-50 is immunologically unrelated to 30-kDa protein, a previously described bundling protein from Dictyostelium. Immunofluorescence with affinity-purified polyclonal antibodies indicates that ABP-50 is localized in regions of the amoeboid cell cortex containing actin bundles. The molar ratio of ABP-50 to actin is approximately 1:5 in vivo. Therefore, the abundance of ABP-50 suggests that it may be responsible for the majority of the bundling activity in these cells.