Markey F, Larsson H, Weber K, Lindberg U
Biochim Biophys Acta. 1982 May 21;704(1):43-51. doi: 10.1016/0167-4838(82)90130-3.
The lag in polymerization of calf spleen profilactin in response to addition of MgCl2 can be overcome by small amounts of spectrin-actin-band 4.1 complex, covalently crosslinked actin oligomers or sonicated F-actin. All of these factors also nucleate polymerization of pure actin. Another nucleator of actin polymerization, villin, delays filaments formation from profilactin. A simple model of the interaction of profilin with actin can explain these apparently conflicting results in terms of the polarity with which actin filaments elongate from the different nuclei.
添加MgCl₂后，小牛脾肌动蛋白原聚合反应的延迟可被少量血影蛋白-肌动蛋白-4.1带复合物、共价交联的肌动蛋白寡聚体或超声处理的F-肌动蛋白克服。所有这些因素也能引发纯肌动蛋白的聚合。另一种肌动蛋白聚合的成核剂——绒毛蛋白，会延迟肌动蛋白原形成细丝。肌动蛋白结合蛋白与肌动蛋白相互作用的一个简单模型，可以根据肌动蛋白丝从不同核延伸的极性来解释这些明显相互矛盾的结果。
