Nishida E, Kuwaki T, Maekawa S, Sakai H
J Biochem. 1981 May;89(5):1655-8. doi: 10.1093/oxfordjournals.jbchem.a133363.
A new protein factor that regulates the state of actin polymerization was purified from porcine brain by DNase I-agarose chromatography. The purified protein factor consisted of a 1 : 1 complex of 88,000 dalton polypeptide and actin. When actin was polymerized by salt in the presence of the factor, the steady-state viscosity and the sedimentability were greatly reduced. The extent of the reductions was found to be greater in the presence of Ca2+ than in its absence.
通过脱氧核糖核酸酶I -琼脂糖层析法从猪脑中纯化出一种调节肌动蛋白聚合状态的新蛋白质因子。纯化后的蛋白质因子由一个88,000道尔顿的多肽与肌动蛋白按1:1比例形成的复合物组成。当在该因子存在的情况下通过盐使肌动蛋白聚合时，稳态粘度和沉降性大大降低。结果发现，在有Ca2+存在时降低的程度比没有Ca2+时更大。
