γ-Glutamylcysteine synthetase from erythrocytes
γ-Glutamylcysteine synthetase from erythrocytes
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来自红细胞的γ-谷氨酰半胱氨酸合成酶
DOI：
10.1016/0003-2697(84)90079-4
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发表时间：
1984
影响因子：
2.9
通讯作者：
A. Meister
中科院分区：
文献类型：
--
作者：
G. Seelig;A. Meister
用三步法从大鼠红细胞中分离得到活性高(比活力约1400U/mg)、均一的γ-谷氨酰半胱氨酸合成酶。该酶的相对分子质量约为100,000，由两个亚基(Mr∼75,000和25,000)组成。红细胞酶表现出与大鼠肾脏γ-谷氨酰半胱氨酸合成酶非常相似的物理化学、催化和免疫学特性。本文所述的分离程序也成功地应用于从绵羊红细胞中分离该酶，这可能有助于探索该酶突变形式的性质。
γ-Glutamylcysteine synthetase was isolated by means of a three-step method in highly active (specific activity, about 1400 units/mg) and apparently homogeneous form from rat erythrocytes. The enzyme has a molecular weight of about 100,000, and is composed of two subunits (Mr∼ 75,000 and 25,000). The erythrocyte enzyme exhibits physicochemical, catalytic, and immunological properties that closely resemble those displayed by rat kidney γ-glutamylcysteine synthetase. The isolation procedure described here, which was also successfully applied to isolation of the enzyme from sheep erythrocytes, may be useful in exploring the properties of mutant forms of the enzyme.