Gitelman S E, Witman G B
J Cell Biol. 1980 Dec;87(3 Pt 1):764-70. doi: 10.1083/jcb.87.3.764.
Calmodulin has been purified from cell bodies of the green alga Chlamydomonas by Ca++-dependent affinity chromatography on fluphenazine-Sepharose 4B. Calmodulin from this primitive organism closely resembles that from bovine brain in a number of properties, including (a) binding to fluphenazine in a Ca++-dependent, reversible manner, (b) functioning as a heat-stable, Ca++-dependent activator of cyclic nucleotide phosphodiesterase, and (c) electrophoretic mobility in SDS-polyacrylamide gels in both the presence and absence of Ca++, which causes a shift in the relative mobility of calmodulin. Calmodulin has also been identified by the criteria of phosphodiesterase activation and electrophoretic mobility in both the detergent soluble "membrane plus matrix" and the axoneme fractions of Chlamydomonas flagella. Calmodulin is not associated with the partially purified 12S or 18S dynein ATPases of Chlamydomonas. The presence of calmodulin in the flagellum suggests that it is involved in one or more of the Ca++-dependent activities of this organelle.
通过在氟奋乃静 - 琼脂糖4B上进行钙离子依赖的亲和层析，从绿藻衣藻的细胞体中纯化出了钙调蛋白。这种原始生物中的钙调蛋白在许多特性上与牛脑中的钙调蛋白非常相似，包括：（a）以钙离子依赖的、可逆的方式与氟奋乃静结合；（b）作为一种热稳定的、钙离子依赖的环核苷酸磷酸二酯酶激活剂发挥作用；（c）在有无钙离子的情况下，在SDS - 聚丙烯酰胺凝胶中的电泳迁移率，钙离子会导致钙调蛋白相对迁移率发生变化。通过磷酸二酯酶激活和电泳迁移率的标准，在衣藻鞭毛的去污剂可溶的“膜加基质”和轴丝部分中也鉴定出了钙调蛋白。钙调蛋白与衣藻部分纯化的12S或18S动力蛋白ATP酶不相关。鞭毛中钙调蛋白的存在表明它参与了该细胞器的一种或多种钙离子依赖的活动。
