Assembly of proteolytically cleaved tubulin.
Assembly of proteolytically cleaved tubulin.
复制标题
蛋白水解裂解的微管蛋白的组装。
DOI：
10.1016/0003-9861(83)90385-5
复制
发表时间：
1983
影响因子：
3.9
通讯作者：
Erickson,HP
中科院分区：
文献类型：
--
作者：
Brown,HR;Erickson,HP
已经发现了纯化的微管蛋白的有限蛋白水解的条件，其中70-90%的分子在一个或两个位点被切割。嗜热菌蛋白酶和胰凝乳蛋白酶分别在单个位点切割α和β亚基。胰蛋白酶在两个位点切割α亚基。胰凝乳蛋白酶网站和胰蛋白酶网站之一，显然是不可访问的组装微管。不同的微管蛋白样品在含有1 m谷氨酸钠的缓冲液中完全能够组装。在另一种缓冲液（50 mmmorpholinoethanesulfonic acid，3.4mglycerol）中，由嗜热菌蛋白酶消化的微管蛋白与天然微管蛋白一样组装，但由胰凝乳蛋白酶或胰蛋白酶消化的样品即使在高蛋白浓度下也不会组装。
Conditions have been found for limited proteolysis of purified tubulin, in which 70–90% of the molecules are cleaved at one or two sites. Thermolysin and chymotrypsin cleave the alpha and beta subunits, respectively, at single sites. Trypsin cleaves the alpha subunit at two sites. The chymotrypsin site and one of the trypsin sites are apparently inaccessible on assembled microtubules. The different samples of proteolyzed tubulin were all fully competent to assemble in a buffer containing 1msodium glutamate. In another buffer (50 mmmorpholinoethanesulfonic acid, 3.4mglycerol) tubulin digested by thermolysin assembled as well as native tubulin, but samples digested by chymotrypsin or trypsin would not assemble even at high protein concentrations.