Podgornaia O I, Drozdov A D, Pinaev G P
Biokhimiia. 1981 Jun;46(6):1015-25.
In gelatinated extracts of starfish ambulacral podia the actin polymerized during gel formation exists as oligomers incapable of binding to rabbit myosin. Actin is also the major protein extractable from the cells by glycerol- and Triton-containing solutions, which do not destroy the contractile mechanism of the cells. The weakly bound gel proteins washed from gel by low ionic strength solutions comprise a factor hampering the polymerization of rabbit actin. The data obtained suggest that the ambulacral sarcoplasmic proteins contain actin (profilament form) coupled to the factor preventing its polymerization.
在海星步带足的凝胶状提取物中，凝胶形成过程中聚合的肌动蛋白以寡聚体形式存在，无法与兔肌球蛋白结合。肌动蛋白也是细胞中可被含甘油和 Triton 的溶液提取的主要蛋白质，这些溶液不会破坏细胞的收缩机制。通过低离子强度溶液从凝胶中洗脱出的弱结合凝胶蛋白包含一种阻碍兔肌动蛋白聚合的因子。所得数据表明，步带肌浆蛋白含有与阻止其聚合的因子偶联的肌动蛋白（原纤维形式）。
