Purification of GTPase-activating protein specific for the rho gene products.
Purification of GTPase-activating protein specific for the rho gene products.
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纯化 rho 基因产物特异的 GTP 酶激活蛋白。
DOI：
10.1016/s0021-9258(20)89496-4
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发表时间：
1991
期刊：
影响因子：
--
通讯作者：
S. Narumiya
中科院分区：
文献类型：
--
作者：
N. Morii;K. Kawano;A. Sekine;T. Yamada;S. Narumiya
从牛肾上腺胞浆中纯化出一种对rho基因产物具有特异性的GTP酶激活蛋白（rho-GAP）。纯化步骤包括硫酸铵分级分离、苯基-琼脂糖和CM-Sepharose柱层析、TSK-凝胶G3000 SW凝胶过滤和Mono S快速蛋白液相色谱。通过这些方法，活性纯化了约36，000倍，回收率为0.6%。最终制备物在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上在Mr 28，000处显示出主要蛋白条带，并以时间和剂量依赖性方式通过纯化的rho A蛋白刺激GTP水解。对ras p21无刺激作用。由肉毒杆菌C3外切酶对rho蛋白的ADP-核糖基化不影响其与纯化的rho-GAP的相互作用。
A GTPase-activating protein specific for the rho gene products (rho-GAP) was purified from the cytosol of bovine adrenal gland. Purification procedures consisted of ammonium sulfate fractionation, chromatographies on columns of phenyl-Sepharose and CM-Sepharose, gel filtration on a TSK-gel G3000SW, and Mono S fast protein liquid chromatography. By these procedures the activity was purified about 36,000-fold with a recovery of 0.6%. The final preparation showed a major protein band at Mr 28,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and stimulated GTP hydrolysis by the purified rho A protein in a time- and dose-dependent manner. No stimulation was found for ras p21. The ADP-ribosylation on the rho protein by botulinum C3 exoenzyme did not affect its interaction with the purified rho-GAP.
影响因子：
4.1
作者：
Gibson, RM;Wilson-Delfosse, AL
通讯作者：
Wilson-Delfosse, AL