...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >beta-tubulin isotypes purified from bovine brain have different relative stabilities
【24h】

beta-tubulin isotypes purified from bovine brain have different relative stabilities

机译：从牛脑纯化的β-微管蛋白同种型具有不同的相对稳定性

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

The highly conserved nature and tissue specificity of the seven vertebrate beta-tubulin isotypes provide circumstantial evidence that functional differences among isotypes may exist in vivo. Compelling evidence from studies of bovine brain beta-isotypes indicated significant conformational and functional differences in vitro and implied that these differences could be related to in vivo function. A previously uninvestigated parameter of potential importance in assessing functional significance is molecular stability. We examined the relative stability of alpha beta(II) and alpha beta(III) tubulin dimers purified from bovine brain. The use of probes to monitor the exposure of hydrophobic areas and sulfhydryls and the loss of colchicine binding, all of which are known to accompany tubulin's time-dependent loss of function, showed an acceleration of these criteria in alpha beta(II) relative to alpha beta(III) when the isotypes were incubated at 37 degrees C. Studies using differential scanning calorimetry suggested that unfolding of the isotypes at similar to 60 degrees C and decay at 0 degrees C were both highly cooperative. It was also observed that alpha beta(III) had a higher melting temperature and a larger population of molecules retaining tertiary structure after incubation at 0 degrees C for 20 h. These studies support the conclusion that alpha beta(III) is significantly more stable than alpha beta(II) and raise the possibility that differences in relative stabilities of tubulin isotypes may be important in regulating the functional properties of microtubules in vivo. [References: 34]
机译：七个脊椎动物β-微管蛋白同种型的高度保守的性质和组织特异性提供了间接证据，表明同种型之间的功能差异可能在体内存在。牛脑β同种型研究的有力证据表明，体外构象和功能存在显着差异，并暗示这些差异可能与体内功能有关。在评估功能重要性方面潜在的先前尚未研究的参数是分子稳定性。我们检查了从牛脑中纯化的α-β（II）和α-β（III）微管蛋白二聚体的相对稳定性。使用探针监测疏水区和巯基的暴露以及秋水仙碱结合的丧失（已知所有这些都伴随着微管蛋白的时间依赖性功能丧失）显示出相对于alpha而言，这些标准在alpha beta（II）中的加速当同种型在37摄氏度下孵育时，β（III）。使用差示扫描量热法的研究表明，同种型在类似于60摄氏度下的解折叠和在0摄氏度下的衰变都是高度协同的。还观察到，在0摄氏度孵育20小时后，αβ（III）具有更高的熔融温度和更大数量的保留三级结构的分子种群。这些研究支持以下结论：αβ（III）比αβ（II）明显更稳定，并增加了微管蛋白同种型相对稳定性差异对调节体内微管功能特性可能很重要的可能性。 [参考：34]

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