Chen L C, Wu C Y, Chen C F, Chiang C F
Department of Pharmacology, National Yang-Ming University, Taipei, Taiwan, Republic of China.
Prep Biochem. 1995 Nov;25(4):183-95. doi: 10.1080/10826069508010120.
The chlorpromazine-sensitive GTPase from the cell membrane of rat cerebral cortex was purified to homogenity by using DEAE Bio-Gel A agarose, hydroxyapatite and heparin agarose chromatography. The purified chlorpromazine-sensitive GTPase was purified 370-fold to obtain a final specific activity of 40 mumol GTP hydrolyzed2min/mg protein. The purified enzyme was inhibited by chlorpromazine but not by compound 48/80. Magnesium was required for its activity instead of calcium. The purified enzyme had an apparent pH optimum of 8.0, and molecular weight was estimated to be 58,000.
通过使用DEAE生物凝胶A琼脂糖、羟基磷灰石和肝素琼脂糖色谱法，将来自大鼠大脑皮质细胞膜的对氯丙嗪敏感的GTP酶纯化至同质。纯化后的对氯丙嗪敏感的GTP酶纯化了370倍，最终比活性为40 μmol GTP水解/2分钟/毫克蛋白质。纯化后的酶被氯丙嗪抑制，但不被化合物48/80抑制。其活性需要镁而非钙。纯化后的酶的最适pH值明显为8.0，分子量估计为58,000。
