Kaetzel M A, Dedman J R
J Biol Chem. 1987 Feb 5;262(4):1818-22.
A high-affinity calcium-dependent calmodulin-binding protein (CaMBP) has been isolated from Electrophorus electricus main electric organ. This 55-kDa CaMBP has been purified to homogeneity by ion exchange and calmodulin-Sepharose affinity chromatography and electrophoretic elution from preparative sodium dodecyl sulfate-polyacrylamide gels. Antibodies against the 55-kDa CaMBP were raised in sheep and were affinity purified. A 47-kDa high-affinity CaMBP species was demonstrated by limited protease digestion and immunoblot analysis to be derived from the 55-kDa CaMBP. The 55-kDa CaMBP has also been isolated from skeletal muscle. It is not detectable by immunoblot analysis in nonexcitable tissues. Characterization of the 55-kDa high-affinity calmodulin-acceptor protein may further elucidate the role of calcium-calmodulin in the regulation of bioelectricity.
一种高亲和力的钙依赖性钙调蛋白结合蛋白（CaMBP）已从电鳗的主要电器官中分离出来。这种55 kDa的CaMBP通过离子交换、钙调蛋白-琼脂糖亲和色谱以及从制备性十二烷基硫酸钠-聚丙烯酰胺凝胶上进行电泳洗脱，已被纯化至同质状态。针对55 kDa CaMBP的抗体在绵羊体内产生并进行了亲和纯化。通过有限的蛋白酶消化和免疫印迹分析表明，一种47 kDa的高亲和力CaMBP是由55 kDa的CaMBP衍生而来。55 kDa的CaMBP也已从骨骼肌中分离出来。在非兴奋性组织中通过免疫印迹分析无法检测到它。对55 kDa高亲和力钙调蛋白受体蛋白的特性研究可能会进一步阐明钙-钙调蛋白在生物电调节中的作用。
