Molecular forms of human-liver arginase

Luz Bascur, Julio Cabello, Marta Véliz, Adriana González
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引用次数: 36

Abstract

The chromatography of liver homogenates and purified preparations of human-liver arginase (l-arginine ureohydrolase, EC 3.5.3.1) on CM-cellulose separates two protein fractions with arginase activity. On rechromatography, each of these fractions appears homogeneous and retains its adsorption-elution characteristics.

Both arginase fractions have similar properties as far as their affinities for substrates, pH optima and thermal inactivation are concerned. However, they differ in their pH stabilities and in their inhibition by ornithine and canavanine.

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人肝精氨酸酶的分子形式
对人肝精氨酸酶(l-精氨酸脲水解酶,EC 3.5.3.1)的肝脏匀浆和纯化制剂在cm -纤维素上进行层析,分离出具有精氨酸酶活性的两个蛋白组分。在重层析上,这些馏分中的每一个看起来都是均匀的,并保持其吸附-洗脱特性。两种精氨酸酶组分在对底物的亲和力、pH最优值和热失活方面具有相似的性质。然而,它们在pH稳定性和对鸟氨酸和大麻氨酸的抑制作用方面有所不同。
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