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出 处:《生物化学杂志》1992年第3期267-271,共5页
摘 要:在Ca^(2+)存在下,肌钙蛋白C(TnC)和肌钙蛋白Ⅰ(TnⅠ)可于高浓度的尿素溶液中形成稳定的复合体,而该复合体又能被EGTA解离。并且TnC和TnⅠ的Ca^(2+)依赖性结合反应没有种间或者肌肉类型间的特异性。将提纯的兔快肌TnC和活化的琼脂糖凝胶进行偶联,制备TnC-Sepharose 4B亲和层析柱,用来从人心肌中直接提纯心脏特异性肌钙蛋白Ⅰ(CSTnⅠ)。SDS-PAGE测得其分子量为29kD左右。对其氨基酸组成亦进行了分析。In the presence of Ca2+, troponin C(TnC) and troponin I(Tn I ) form a specific binary complex that is stable in high urea concentration and which can be dissociated by ethanedeoxybis- (ethylamine) tetra-acetic acid (EGTA) .Moreover, there is no species or muscle type specificity of Ca2+-dependent interaction between TnC and Tn I .Linking the TnC purified from rabbit fast skeletal muscle with activated agarose gel, TnC-Sepharose 4B affinity chromatographic column was developed for the isolation of CSTn I directly from human heart muscle.The result from SDS-PAGE of isolated CSTn I shows that the molecular weight is about 29kD.The amino acid composition of Tn I was also analysed.
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