IDENTIFICATION OF A FACTOR IN CONVENTIONAL MUSCLE ACTIN PREPARATIONS WHICH INHIBITS ACTIN FILAMENT SELF-ASSOCIATION
IDENTIFICATION OF A FACTOR IN CONVENTIONAL MUSCLE ACTIN PREPARATIONS WHICH INHIBITS ACTIN FILAMENT SELF-ASSOCIATION
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DOI：
10.1016/0006-291x(80)91175-4
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发表时间：
1980-01-01
影响因子：
3.1
通讯作者：
POLLARD, TD
中科院分区：
文献类型：
--
作者：
MACLEANFLETCHER, S;POLLARD, TD
解聚的常规纯化的[鸡或兔]肌肉肌动蛋白的凝胶过滤从肌动蛋白单体中分离出一部分斯托克斯半径为4.7 nm的少量污染物，其具有阻断肌动蛋白丝网络形成的能力。根据对热和胰蛋白酶的敏感性，这种抑制活性似乎是一种蛋白质。抑制活性结合到肌动蛋白丝和降低其低剪切粘度高达99%，在浓度依赖性的方式，同时减少聚合到一个较小的程度。
Gel filtration of depolymerized conventionally purified [chicken or rabbit] muscle actin separates from the actin monomers a fraction of minor contaminants with a stokes'' radius of 4.7 nm which has the ability to block actin filament network formation. On the basis of heat and trypsin sensitivity, this inhibitory activity appears to be a protein. The inhibitory activity binds to actin filaments and reduces their low shear viscosity by up to 99% in a concentration dependent fashion while reducing polymerization to a minor extent.