Interaction of myotoxin a with the Ca2+-ATPase of skeletal muscle sarcoplasmic reticulum.
Interaction of myotoxin a with the Ca2+-ATPase of skeletal muscle sarcoplasmic reticulum.
复制标题
肌毒素 a 与骨骼肌肌浆网 Ca2-ATP 酶的相互作用。
DOI：
10.1016/0003-9861(86)90452-2
复制
发表时间：
1986
影响因子：
3.9
通讯作者：
Tu,AT
中科院分区：
文献类型：
--
作者：
Volpe,P;Damiani,E;Maurer,A;Tu,AT
肌肉毒素是一种从响尾蛇毒液中分离出来的肌肉损伤毒素。研究了它与兔骨骼肌肌浆网囊泡Ca ~（2+）-ATP酶的相互作用。Myotoxin抑制Ca ~（2+）负荷，刺激Ca ~（2+）依赖的ATP酶，但不影响Ca ~（2+）的单向流出。其作用具有剂量、时间和温度依赖性。肌毒素部分阻断特异性抗（兔SR Ca 2 +-ATP酶）抗体的结合。肌毒素与肌浆网Ca ~（2+）-ATP酶结合，使Ca ~（2+）摄取与依赖Ca ~（2+）的ATP水解不偶联。肌毒素也阻止了十钒酸钠诱导的SR Ca ~（22+）-ATP酶二维晶体阵列的形成。
Myotoxinais a muscle-damaging toxin isolated from the venom ofCrotalus viridis viridis. Its interaction with the Ca2+-ATPase of sarcoplasmic reticulum (SR) vesicles purified from rabbit skeletal muscle was investigated. Myotoxinainhibited Ca2+loading and stimulated Ca2+-dependent ATPase without affecting unidirectional Ca2+efflux. Its action was dose, time, and temperature dependent. Myotoxinapartially blocked the binding of specific anti-(rabbit SR Ca2+-ATPase) antibodies. It is concluded that myotoxinaattaches to the SR Ca2+-ATPase and uncouples Ca2+uptake from Ca2+-dependent ATP hydrolysis. Myotoxinaalso prevented the formation of decavanadate-induced two-dimensional crystalline arrays of the SR Ca22+-ATPase.