Kawashima A, Shiraishi F, Ohtsuki I, Yamamoto K
Department of Clinical Pharmacology, Faculty of Medicine, Kyushu University, Fukuoka, Japan.
Mol Cell Biochem. 1994 Mar 30;132(2):173-7. doi: 10.1007/BF00926926.
In order to compare the role of the Ca(2+)-receptive protein (troponin), in the characteristic myofibrillar contractile response of chicken fast and slow skeletal muscles, the troponin in both kinds of myofibrils were partially exchanged, under slightly acidic conditions. The Ca(2+)- or Sr(2+)-activation of the ATPase of fast (or slow) skeletal myofibrils hybridized with slow (or fast) skeletal troponin profiles were also investigated. The results indicated that the Ca(2+)- or Sr(2+)-affinity of the myofibrillar ATPase activity were related to the species of troponin. This procedure for replacing troponin in myofibrils under physiological conditions is thus considered to be useful for the study of the Ca(2+)-regulatory mechanism in myofibrillar contraction.
为了比较钙受体蛋白(肌钙蛋白)在鸡快、慢骨骼肌肌原纤维特征性收缩反应中的作用,在微酸性条件下,对两种肌原纤维中的肌钙蛋白进行了部分交换。还研究了与慢(或快)骨骼肌肌钙蛋白杂交的快(或慢)骨骼肌肌原纤维ATP酶的钙(或锶)激活情况。结果表明,肌原纤维ATP酶活性的钙(或锶)亲和力与肌钙蛋白的种类有关。因此,这种在生理条件下替换肌原纤维中肌钙蛋白的方法被认为对研究肌原纤维收缩中的钙调节机制有用。