Tumminia S J, Koretz J F, Landau J V
Center for Biophysics, Rensselaer Polytechnic Institute, Troy, NY 12180-3590.
Biochim Biophys Acta. 1990 Sep 27;1040(3):373-81. doi: 10.1016/0167-4838(90)90135-3.
Native thick filaments isolated from freshly prepared rabbit psoas muscle were found to be resistant to pressure-induced dissociation. With increasing pressure application and release, a bimodal distribution of filament lengths was observed. The shorter filament length is associated with filament breakage at the center of the bare zone, while the longer length is associated with relatively intact filaments. Intact filaments and filament halves decrease in length by no more than 20% after exposure to and release of 14,000 psi. Bimodal distributions were not observed in equivalent experiments performed on filaments isolated from muscle glycerinated and stored at -20 degrees C for 6 months. Instead, filament dissociation proceeds linearly as a function of increasing pressure. Filaments prepared from muscle glycerinated and stored for 2 and 4 months exhibited pressure-induced behavior intermediate between the filaments prepared from fresh muscle and filaments prepared from muscle stored for 6 months. Since there appears to be no difference in the protein profiles of the various muscle samples, it is possible that stabilization of the native thick filament against hydrostatic pressure arises from trapped ions that are leached out over time.
从新鲜制备的兔腰大肌中分离出的天然粗肌丝被发现对压力诱导的解离具有抗性。随着压力施加和释放的增加,观察到肌丝长度的双峰分布。较短的肌丝长度与裸区中心的肌丝断裂有关,而较长的长度与相对完整的肌丝有关。完整的肌丝和半肌丝在暴露于14,000 psi并释放后长度减少不超过20%。在对从甘油化肌肉中分离并在-20℃下储存6个月的肌丝进行的等效实验中未观察到双峰分布。相反,肌丝解离随着压力增加呈线性进行。从甘油化肌肉中制备并储存2个月和4个月的肌丝表现出的压力诱导行为介于从新鲜肌肉制备的肌丝和从储存6个月的肌肉制备的肌丝之间。由于各种肌肉样品的蛋白质谱似乎没有差异,因此天然粗肌丝对静水压力的稳定性可能源于随着时间推移被浸出的捕获离子。