On the use of heat stability as a criterion for the identification of microtubule associated proteins (MAPs).
On the use of heat stability as a criterion for the identification of microtubule associated proteins (MAPs).
复制标题
关于使用热稳定性作为鉴定微管相关蛋白（MAP）的标准。
DOI：
10.1016/0006-291x(85)91850-9
复制
发表时间：
1985
影响因子：
3.1
通讯作者：
Vallee,RB
中科院分区：
文献类型：
--
作者：
Vallee,RB
在高温下的溶解度是有限数量的已知微管相关蛋白质所表现出的显著的生物化学性质。这一特性在这些蛋白质的鉴定和纯化中非常有用。本文报道，热稳定性是暴露于高温期间存在的蛋白质组成的函数。所有的非微管蛋白的蛋白质在牛微管制备被发现保持可溶性时，微管蛋白被删除之前加热。向制备物中加入纯化的微管蛋白或牛血清白蛋白恢复了通常在微管蛋白制备物中观察到的选择性热稳定性。
Solubility at elevated temperature is a striking biochemical property exhibited by a restricted number of the known microtubule associated proteins. This property has been extremely useful in the identification of these proteins and in their purification as well. It is reported here that heat stability is a function of the composition of proteins present during exposure to elevated temperature. All non-tubulin proteins in bovine microtubule preparations were found to remain soluble when tubulin was removed prior to heating. Addition of purified tubulin or bovine serum albumin to the preparation restored the selective heat stability normally seen in microtubule protein preparations.