Purification of phospholipase C from rat cerebral cortex.

C Y Wu, C F Chen, C F Chiang
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引用次数: 1

Abstract

Phospholipase C from rat cerebral cortex was purified to homogeneity by use of DEAE Bio-Gel A agarose, hydroxyapatite, and heparin agarose chromatography. The purified phospholipase C (PLC) was purified 622.4-fold and its molecular weight is estimated to be 97,500. We obtained a final specific activity of 3.112 mumol of phosphatidylinositol hydrolyzed/min/mg of protein. It is specific for inositol phospholipids. The purified enzyme has an apparent optimum pH 7.0. Calcium is required for its activity. Western blotting analysis showed that two proteins were recognized by anti-PLC antiserum.

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大鼠大脑皮层磷脂酶C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磷脂酶C。纯化的磷脂酶C (PLC)纯度为622.4倍,分子量估计为97500。最终比活性为3.112 μ mol /min/mg蛋白质水解磷脂酰肌醇。它是针对肌醇磷脂的。纯化酶的最适pH值为7.0。它的活性需要钙。Western blotting分析显示,抗plc抗血清能识别这两种蛋白。
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