肌动蛋白结合蛋白对肌动蛋白沉降特性的影响。
Effect of actin-binding protein on the sedimentation properties of actin.
作者信息
Rosenberg S, Stracher A
出版信息
J Cell Biol. 1982 Jul;94(1):51-5. doi: 10.1083/jcb.94.1.51.
Actin and actin-binding protein (ABP) have recently been purified from human platelet cytoskeletons (S. Rosenberg, A. Stracher, and R.C. Lucas, 1981, J. Cell Biol. 91:201-211). Here, the effect of ABP on the sedimentation of actin was studied. When ABP was added to preformed F-actin filaments, it bound until a maximum ratio of 1:9 (ABP:actin, mol:mol) was reached. however, when actin was polymerized in the presence of ABP, two and a half times more ABP was able to bind to the actin- that is, every 3.4 actin monomers were now bound by an ABP dimer. ABP was not able to induce the sedimentation of actin under nonpolymerizing conditions but was able to reduce the time and concentration of actin required for sedimentation under slow polymerizing conditions. ABP, therefore, exerts its effect of G-actin by either nucleating polymerization or by cross-linking newly formed oligomers into a more sedimentable form.
肌动蛋白和肌动蛋白结合蛋白（ABP）最近已从人血小板细胞骨架中纯化出来（S. 罗森伯格、A. 斯特拉彻和R.C. 卢卡斯，1981年，《细胞生物学杂志》91:201 - 211）。在此，研究了ABP对肌动蛋白沉降的影响。当将ABP添加到预先形成的F - 肌动蛋白丝中时，它会结合，直到达到最大比例1:9（ABP:肌动蛋白，摩尔:摩尔）。然而，当肌动蛋白在ABP存在下聚合时，能够结合到肌动蛋白上的ABP多了两倍半，也就是说，现在每3.4个肌动蛋白单体被一个ABP二聚体结合。在非聚合条件下，ABP不能诱导肌动蛋白沉降，但在缓慢聚合条件下，它能够减少肌动蛋白沉降所需的时间和浓度。因此，ABP通过成核聚合或将新形成的寡聚体交联成更易沉降的形式来发挥其对G - 肌动蛋白的作用。
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