...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Behavior of caldesmon upon interaction of thin filaments with myosin subfragment 1 in ghost fibers
【24h】

Behavior of caldesmon upon interaction of thin filaments with myosin subfragment 1 in ghost fibers

机译：Caldesmon在细丝与肌球蛋白亚片段1在鬼纤维中相互作用时的行为

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Caldesmon is a component of smooth muscle thin filaments which inhibits their interaction with myosin. We have used polarized fluorescence technique to study the behavior of caldesmon during the interaction of myosin subfragment 1 (S1) with thin filaments reconstituted in rabbit skeletal muscle ghost fibers by incorporation of smooth muscle tropomyosin and caldesmon labeled with acrylodan at cysteine residue located in the C-terminal region. Significant changes in acrylodan fluorescence intensity upon addition of skeletal muscle S1 reflected substantial displacement of caldesmon from thin filaments, while alterations in the calculated fluorescence parameters indicated the simultaneous rearrangement of the remaining caldesmon fraction. The orientation of caldesmon in the S1-thin filament complex relative to the fiber axis changes by approximately 7° and the mobility of the fluorescent probe by about 9%. The alterations in caldesmon orientation were proportional to the strength of S1 binding and diminished respectively upon addition of ADP and ADP-V_i. The changes in orientation of acrylodan-caldesmon evoked by the interaction of S1 with thin filaments were more pronounced than that in AEDANS-F-actin which suggests that the spatial arrangement of caldesmon in the complex is governed not only by F-actin but also by S1. The results may indicate that the changes in spatial arrangement of caldesmon are adjusted to the conformation of F-actin and S1 characteristic for particular steps of the ATP hydrolysis cycle.
机译：Caldesmon是平滑肌细丝的成分，可抑制细丝与肌球蛋白的相互作用。我们使用偏振荧光技术研究了肌球蛋白亚片段1（S1）与兔骨骼肌鬼影纤维中重构的细丝相互作用时卡尔德斯蒙的行为，方法是在C的半胱氨酸残基上掺入平滑肌原肌球蛋白和用丙烯酰胺标记的卡尔德斯蒙。 -末端区域。添加骨骼肌S1后，丙烯醛荧光强度的显着变化反映了Caldesmon从细细丝上的大量置换，而计算的荧光参数发生变化则表明剩余Caldesmon分数同时发生了重排。 Caldesmon在S1细丝络合物中相对于纤维轴的方向变化约7°，荧光探针的迁移率变化约9％。 Caldesmon取向的变化与S1结合的强度成正比，并在加入ADP和ADP-V_1后分别减弱。 S1与细丝的相互作用引起的丙烯酰胺-卡尔德斯蒙取向变化比AEDANS-F-肌动蛋白更明显，这表明卡尔德斯蒙在复合物中的空间排列不仅受F-肌动蛋白的控制，而且还受其影响。 S1结果可能表明，对于ATP水解循环的特定步骤，卡尔德斯蒙的空间排列变化已根据F-肌动蛋白的构象和S1特征进行了调整。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号