Connell J P, Mullet J E
Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843.
Plant Physiol. 1986 Oct;82(2):351-6. doi: 10.1104/pp.82.2.351.
Glutathione reductase (EC 1.6.4.2) was purified from intact pea (Pisum sativum) chloroplasts by a method which includes affinity chromatography on ADP-agarose. Fractions from the affinity column which had glutathione reductase activity consisted of polypeptides of 60 and 32 kilodaltons. Separation of the proteins by electrophoresis on native gels showed that glutathione reductase activity was associated with 60 kilodalton polypeptides and not with the 32 kilodalton polypeptides. Antibodies to spinach whole leaf glutathione reductase (60 kilodaltons) cross-react with the chloroplast 60 kilodalton glutathione reductase but not the 32 kilodalton polypeptides. In the absence of dithiothreitol the 60 kilodalton polypeptides showed a shift in apparent molecular weight on sodium dodecyl sulfate gels to 72 kilodaltons. Dithiothreitol did not alter the activity of the chloroplast enzyme. Chloroplast glutathione reductase is relatively insensitive to NADPH.
谷胱甘肽还原酶（EC 1.6.4.2）通过一种包括在ADP-琼脂糖上进行亲和层析的方法从完整的豌豆（Pisum sativum）叶绿体中纯化得到。亲和柱上具有谷胱甘肽还原酶活性的组分由60千道尔顿和32千道尔顿的多肽组成。通过在天然凝胶上进行电泳分离蛋白质表明，谷胱甘肽还原酶活性与60千道尔顿的多肽相关，而与32千道尔顿的多肽无关。针对菠菜全叶谷胱甘肽还原酶（60千道尔顿）的抗体与叶绿体60千道尔顿的谷胱甘肽还原酶发生交叉反应，但不与32千道尔顿的多肽发生反应。在没有二硫苏糖醇的情况下，60千道尔顿的多肽在十二烷基硫酸钠凝胶上的表观分子量向72千道尔顿移动。二硫苏糖醇不会改变叶绿体酶的活性。叶绿体谷胱甘肽还原酶对NADPH相对不敏感。
Zotero 插件
