Seelig G F, Meister A
Anal Biochem. 1984 Sep;141(2):510-4. doi: 10.1016/0003-2697(84)90079-4.
gamma-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 approximately 75,000 and 25,000). The erythrocyte enzyme exhibits physicochemical, catalytic, and immunological properties that closely resemble those displayed by rat kidney gamma-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.
通过三步法从大鼠红细胞中分离出了γ-谷氨酰半胱氨酸合成酶，其活性很高（比活性约为1400单位/毫克），且呈明显的均一形式。该酶的分子量约为100,000，由两个亚基组成（分子量分别约为75,000和25,000）。红细胞中的这种酶在物理化学、催化和免疫学性质方面与大鼠肾脏γ-谷氨酰半胱氨酸合成酶极为相似。本文所述的分离方法也成功应用于从绵羊红细胞中分离该酶，可能有助于探索该酶突变形式的性质。
