Purification of chlorpromazine-sensitive GTPase from rat cerebral cortex.

L C Chen, C Y Wu, C F Chen, C F Chiang
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引用次数: 1

Abstract

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.

大鼠大脑皮层氯丙嗪敏感GTPase的纯化。
采用DEAE Bio-Gel A琼脂糖、羟基磷灰石和肝素琼脂糖层析纯化大鼠大脑皮层细胞膜氯丙嗪敏感GTPase至均质。纯化的氯丙嗪敏感GTP酶被纯化370倍,得到GTP水解2min/mg蛋白的最终比活性为40 μ mol。氯丙嗪对纯化酶有抑制作用,而化合物48/80对纯化酶无抑制作用。它的活性需要镁而不是钙。纯化酶的最适pH值为8.0,分子量估计为58000。
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