Marshak D R, Watterson D M, Van Eldik L J
Proc Natl Acad Sci U S A. 1981 Nov;78(11):6793-7. doi: 10.1073/pnas.78.11.6793.
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.
我们通过在吩噻嗪-琼脂糖偶联物上进行基于亲和的吸附色谱法纯化了脑特异性蛋白S100b，并研究了该蛋白及其他钙调节蛋白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S100b以钙依赖的方式与吩噻嗪-琼脂糖结合。这三种蛋白竞争性抑制125I标记的鸡砂囊钙调蛋白与固定化药物的钙依赖性结合。然而，鲤鱼小清蛋白和鸡肠维生素D依赖性钙结合蛋白并不抑制吩噻嗪-钙调蛋白的相互作用。这些结果表明，钙调蛋白、肌钙蛋白C和S100b之间已知的氨基酸序列同源性可能反映在这些蛋白中存在但小清蛋白和维生素D依赖性蛋白中不存在的相似功能域中。
