Jamieson G A, Vanaman T C, Blum J J
Proc Natl Acad Sci U S A. 1979 Dec;76(12):6471-5. doi: 10.1073/pnas.76.12.6471.
Ca-dependent affinity chromatography on phenothiazine-Sepharose 4B has been used to isolate a pure protein from the ciliate Tetrahymena pyriformis. This protein has been identified as calmodulin by demonstrating three of the Ca-dependent activities attributed to calmodulins. Tetrahymena calmodulin also has physicochemical properties similar to those of the previously characterized mammalian, coelenterate, and plant proteins, except for a lower molecular weight (15,000) and slightly different CNBr fragments compared to bovine brain calmodulin. Calmodulin is a constituent of demembranated Tetrahymena cilia from which it can be extracted with the crude dynein fraction. Sucrose density gradient fractionation indicated its presence in fractions containing the 14S dynein ATPase. It is concluded that the essential properties of calmodulin have been highly conserved during much of eukaryotic evolution, and it is suggested that calmodulin plays a role in the control of ciliary motility in Tetrahymena.
利用吩噻嗪 - 琼脂糖凝胶4B进行的钙依赖亲和层析已用于从梨形四膜虫中分离出一种纯蛋白。通过证明该蛋白具有三种归因于钙调蛋白的钙依赖活性，已将其鉴定为钙调蛋白。除了分子量较低（15,000）且与牛脑钙调蛋白相比CNBr片段略有不同外，四膜虫钙调蛋白还具有与先前表征的哺乳动物、腔肠动物和植物蛋白相似的物理化学性质。钙调蛋白是去膜四膜虫纤毛的组成成分，可从其中用粗动力蛋白部分提取出来。蔗糖密度梯度分级分离表明它存在于含有14S动力蛋白ATP酶的级分中。得出的结论是，在真核生物进化的大部分过程中，钙调蛋白的基本特性得到了高度保守，并且有人提出钙调蛋白在四膜虫纤毛运动的控制中起作用。
