Johnson R E, Adams P H
FEBS Lett. 1984 Aug 20;174(1):11-4. doi: 10.1016/0014-5793(84)81067-4.
The binding of Mg2+ ADP to both rabbit skeletal and bovine cardiac myofibrils has been studied at two different temperatures. In each case a single class of binding sites was observed with a binding constant very close to that reported for the analogous actomyosin-subfragment one but much weaker than that seen with the analogous myosin subfragment one alone. These findings are discussed in terms of the constraints on the myosin cross-bridges imposed by the regular array of thick and thin filaments found in myofibrils.
已在两种不同温度下研究了Mg2+ ADP与兔骨骼肌和牛心肌肌原纤维的结合情况。在每种情况下,均观察到一类结合位点,其结合常数与报道的类似肌动球蛋白亚片段1的结合常数非常接近,但比单独观察到的类似肌球蛋白亚片段1的结合常数弱得多。根据肌原纤维中粗细肌丝规则排列对肌球蛋白横桥施加的限制来讨论这些发现。