Walter M F, Schultz J E
Eur J Cell Biol. 1981 Apr;24(1):97-100.
A low molecular weight protein of about 17 000 as determined by SDS-polyacrylamide gel electrophoresis has been isolated from cilia and cell bodies, respectively, from Paramecium tetraurelia (wildtyp 51s). This protein has been identified as calmodulin by various properties previously ascribed to calmodulin from other vertebrate and invertebrate systems. These properties are heat stability, electrophoretic mobility and its ability to activate in the presence of calcium a calmodulin-dependent phosphodiesterase from pig brain. Calmodulin is present in rather high amounts in cell bodies (75 micrograms/g) and also in isolated cell-free cilia (up to 50 micrograms/g). Its presence in cilia suggests a role in the control of ciliary activity.
通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定,从四膜虫(野生型51s)的纤毛和细胞体中分别分离出一种分子量约为17000的低分子量蛋白质。根据先前赋予其他脊椎动物和无脊椎动物系统中钙调蛋白的各种特性,该蛋白质已被鉴定为钙调蛋白。这些特性包括热稳定性、电泳迁移率以及在钙存在下激活猪脑钙调蛋白依赖性磷酸二酯酶的能力。钙调蛋白在细胞体中含量相当高(75微克/克),在分离的无细胞纤毛中也有(高达50微克/克)。它在纤毛中的存在表明其在控制纤毛活动中发挥作用。