Calcium-dependent interaction of S100b, troponin C, and calmodulin with an immobilized phenothiazine.
Calcium-dependent interaction of S100b, troponin C, and calmodulin with an immobilized phenothiazine.
复制标题
S100b、肌钙蛋白 C 和钙调蛋白与固定化吩噻嗪的钙依赖性相互作用。
DOI：
10.1073/pnas.78.11.6793
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发表时间：
1981
影响因子：
11.1
通讯作者：
VanEldik,LJ
中科院分区：
文献类型：
--
作者：
Marshak,DR;Watterson,DM;VanEldik,LJ
我们已经纯化了脑特异性蛋白S100 b的亲和吸附层析吩噻嗪-琼脂糖凝胶缀合物，并研究了这种和其他钙调节蛋白质与固定化抗精神病药物的相互作用。牛脑钙调蛋白、兔骨骼肌肌钙蛋白C和牛脑S100 b以钙依赖性方式与吩噻嗪-琼脂糖凝胶结合。这三种蛋白质竞争性地抑制钙依赖性结合125 I-标记的鸡砂囊钙调素的固定化药物。然而，鲤鱼小清蛋白和鸡肠道维生素D依赖性钙结合蛋白不抑制吩噻嗪-钙调素的相互作用。这些结果表明，钙调蛋白，肌钙蛋白C，和S100 b之间的已知氨基酸序列同源性可能反映在一个类似的功能结构域存在于这些蛋白质，但缺乏小清蛋白和维生素D依赖性蛋白。
We have purified the brain-specific protein S100b by affinity-based adsorption chromatography on phenothiazine-Sepharose conjugates and studied the interaction of this and other calcium-modulated proteins with the immobilized antipsychotic drug. Bovine brain calmodulin, rabbit skeletal muscle troponin C, and bovine brain S100b bind to phenothiazine-Sepharose in a calcium-dependent manner. These three proteins competitively inhibit the calcium-dependent binding of 125I-labeled chicken gizzard calmodulin to the immobilized drug. However, carp parvalbumin and chicken intestinal vitamin D-dependent calcium binding protein do not inhibit the phenothiazine--calmodulin interaction. These results suggest that the known amino acid sequence homology among calmodulin, troponin C, and S100b may be reflected in a similar functional domain present in these proteins but absent in parvalbumin and vitamin D-dependent protein.