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关于肌球蛋白ATP酶活性变化与心肌肌球蛋白分子结构之间的关系,尚不完全清楚,但较多的人认为,肌球蛋白ATP酶同工酶的变化是由于肌球蛋白重链变化造成的。此外已知,肌球蛋白的轻链是肌球蛋白分子上的重要亚基,对肌球蛋白ATP酶活性影响甚大。克山病患区粮喂饲的大白鼠心肌肌球蛋白ATP酶活性及同工酶变化与肌球蛋白轻链是否有关,是亟待解决的问题。为此,本实验应用Katagiri法并加以改良、定量地分析了患区粮喂饲大白鼠心肌、中全部结构蛋白。发现在患区粮喂饲的大白鼠心肌中,其心室肌肌球蛋白轻链的比例发生了极为显著的变化。这说明,肌球蛋白ATP酶同工酶的变化,不仅是肌球蛋白重链,而且还有轻链共同参与变化的结果。从而,更深刻地说明了肌球蛋白ATP酶活性变化的原因。
The relationship between changes in myosin ATPase activity and myocardial myosin molecular structure is not fully understood, but more people think that changes in myosin ATPase is due to myosin heavy chain changes Caused. It is also known that the light chain of myosin is an important subunit on the myosin molecule and has a great influence on the myosin ATPase activity. Keshan disease-fed rat myocardial myosin ATPase activity and isoenzyme changes and myosin light chain is related to the problem to be solved. To this end, the experiment using Katagiri method and to be improved, quantitative analysis of the affected area of grain-fed rats myocardium, all the structural proteins. Found in the regional food-fed rat myocardium, the proportion of myosin light chain of ventricular my significant changes have taken place. This shows that changes in myosin ATPase isoenzyme, not only myosin heavy chain, but also light chain involved in the results of changes. Thus, the reason for the change of myosin ATPase activity is further elucidated.