Takahashi K, Kim O H, Yano K
J Biochem. 1987 Mar;101(3):767-73. doi: 10.1093/jb/101.3.767.
The reaction mechanism of calcium ion in the postmortem weakening of Z-disks was studied in myofibrils prepared from fresh or stored muscles. The alpha-actinin content in myofibrils remained almost unchanged within 10 days postmortem, showing very limited proteolysis of myofibrils during postmortem storage of muscles at 10 degrees C. The postmortem weakening of Z-disks was markedly dependent on muscle pH, showing a minimum at pH 6.5. These results agree well with the calcium-induced weakening of Z-disks of freshly isolated myofibrils, indicating that no protease participates in the postmortem weakening of Z-disks. Z-Disks of myofibrils prepared from stored muscles split into halves after treatment with 0.1 N NaOH for 5 min. The identical splitting of Z-disks was induced by a calcium ion concentration of 10(-4)M, which is of the same order of magnitude as that in the sarcoplasm in postmortem muscle. We therefore conclude that the postmortem weakening of Z-disks is non-enzymatically induced by the raised sarcoplasmic calcium ion concentration of 10(-4) M. Calcium ions probably solubilize the amorphous cementing material of Z-disks, leaving unchanged the two sets of Z filaments composed of alpha-actinin.
在从新鲜或储存肌肉制备的肌原纤维中研究了钙离子在Z盘死后弱化中的反应机制。肌原纤维中的α - 辅肌动蛋白含量在死后10天内几乎保持不变,这表明在10℃下肌肉死后储存期间肌原纤维的蛋白水解非常有限。Z盘的死后弱化明显取决于肌肉pH值,在pH 6.5时达到最小值。这些结果与新鲜分离的肌原纤维中钙离子诱导的Z盘弱化非常吻合,表明没有蛋白酶参与Z盘的死后弱化。用0.1 N NaOH处理5分钟后,从储存肌肉制备的肌原纤维的Z盘分成两半。10(-4)M的钙离子浓度诱导了相同的Z盘分裂,这与死后肌肉肌浆中的钙离子浓度处于同一数量级。因此,我们得出结论,Z盘的死后弱化是由肌浆中钙离子浓度升高至10(-4) M非酶促诱导的。钙离子可能使Z盘的无定形胶结物质溶解,而由α - 辅肌动蛋白组成的两组Z细丝保持不变。