Maruyama K, Sakai H
J Biochem. 1981 Apr;89(4):1337-40.
A motility-regulatory protein called cell beta-actinin was isolated from rat kidney cytosol. Although its molecular weight (approximately 80,000) is different from that of beta-actinin from skeletal muscle (heterodimer of 34,000 and 37,000), the action on actin is the same for both. Cell beta-actinin accelerates polymerization of actin by enhanced nucleation resulting in shorter actin filaments, inhibits the reassociation of sonicated F-actin fragments, and forms a Mg polymer in the presence of Mg ions. Cell beta-actinin appears to be present in various tissues of rat, rabbit, chicken, and pig. Cell beta-actinin is thought to function as an accelerator of actin polymerization in nonmuscle cells, in which actin monomers are abundantly present.
一种名为细胞β-辅肌动蛋白的运动调节蛋白是从大鼠肾细胞溶质中分离出来的。尽管其分子量(约80,000)与骨骼肌β-辅肌动蛋白(34,000和37,000的异二聚体)不同,但二者对肌动蛋白的作用是相同的。细胞β-辅肌动蛋白通过增强成核作用加速肌动蛋白的聚合,从而产生更短的肌动蛋白丝,抑制超声处理的F-肌动蛋白片段的重新结合,并在镁离子存在的情况下形成镁聚合物。细胞β-辅肌动蛋白似乎存在于大鼠、兔子、鸡和猪的各种组织中。细胞β-辅肌动蛋白被认为在非肌肉细胞中作为肌动蛋白聚合的促进剂发挥作用,在这些细胞中肌动蛋白单体大量存在。