Kerrick W G, Zot H G, Hoar P E, Potter J D
J Biol Chem. 1985 Dec 15;260(29):15687-93.
Troponin C (TnC) was extracted from skinned skeletal muscle fibers by a method similar to that used previously on myofibrils (Zot, H.G., and Potter, J.D. (1982) J. Biol. Chem. 257, 7678-7683) and replaced with either skeletal (fast-twitch) or cardiac TnC. The relationship between isometric tension and Sr2+ concentration remained essentially the same before removal and after replacement with skeletal or cardiac TnC. Therefore, the origin of the TnC made no difference in the Sr2+ activation properties of the skinned fiber. In contrast, the activation of skinned cardiac fibers is approximately an order of magnitude more sensitive to Sr2+ than skinned skeletal fibers. These results show that the affinity of cardiac TnC for Sr2+ is altered when substituted into skinned skeletal muscle fibers through protein-protein interactions.
肌钙蛋白C(TnC)是通过一种与先前用于肌原纤维的方法类似的方法从去皮骨骼肌纤维中提取的(佐特,H.G.,和波特,J.D.(1982年)《生物化学杂志》257卷,7678 - 7683页),并用骨骼肌(快肌纤维)或心肌TnC进行替换。等长张力与Sr2 + 浓度之间的关系在去除TnC之前以及用骨骼肌或心肌TnC替换之后基本保持不变。因此,TnC的来源对去皮纤维的Sr2 + 激活特性没有影响。相比之下,去皮心肌纤维的激活对Sr2 + 的敏感性大约比去皮骨骼肌纤维高一个数量级。这些结果表明,当通过蛋白质 - 蛋白质相互作用将心肌TnC替换到去皮骨骼肌纤维中时,其对Sr2 + 的亲和力会发生改变。