SUBCELLULAR-DISTRIBUTION OF MULTIPLE FORMS OF GLUTATHIONE-REDUCTASE IN LEAVES OF PEA (PISUM-SATIVUM-L)
SUBCELLULAR-DISTRIBUTION OF MULTIPLE FORMS OF GLUTATHIONE-REDUCTASE IN LEAVES OF PEA (PISUM-SATIVUM-L)
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DOI：
10.1007/bf00194008
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发表时间：
1990-01-01
期刊：
影响因子：
4.3
通讯作者：
MULLINEAUX, PM
中科院分区：
文献类型：
--
作者：
EDWARDS, EA;RAWSTHORNE, S;MULLINEAUX, PM
在十二烷基硫酸钠聚丙烯酰胺凝胶上，来自两到三周龄豌豆 (Pisum sativum L. cv. Birte) 幼苗叶子的纯化谷胱甘肽还原酶 (GR; EC 1.6.4.2) 由一条表观分子量为 55 千道尔顿的单条带表示。通过二维电泳将该多肽解析为多种同工型。原生质体的分级分离和亚细胞器的纯化表明，酶活性与叶绿体、线粒体和细胞质相关（按此顺序，约占总活性的 77%、3% 和 2%）。从纯化的线粒体和叶绿体中分离出多种不同的酶异构体，这些异构体的等电点不同且具有区室特异性。在 Percoll 梯度上与线粒体标记酶细胞色素 C 氧化酶 (EC 1.9.3.1) 共纯化的谷胱甘肽还原酶活性的潜伏期表明该酶位于线粒体内。线粒体谷胱甘肽还原酶活性强烈依赖于 NADPH 而不是 NADH。
On sodium-dodecyl-sulfate polyacrylamide gels, purified glutathione reductase (GR; EC 1.6.4.2) from the leaves of two- to three-week-old pea (Pisum sativum L. cv. Birte) seedlings was represented by a single band with an apparent molecular weight of 55 kilodaltons. This polypeptide was resolved to multiple isoforms by two-dimensional electrophoresis. Fractionation of protoplasts and purification of subcellular organelles has shown that enzyme activity is associated with the chloroplasts, mitochondria and cytosol (in this order, approx. 77%, 3%, and 2% of the total activity). Distinct multiple isoforms of the enzyme, which differed in isoelectric point and were compartment-specific, were resolved from purified mitochondria and chloroplasts. The latency of the glutathione reductase activity which co-purified on Percoll gradients with the mitochondrial marker enzyme, cytochrome-c oxidase (EC 1.9.3.1), indicated that this enzyme was within the mitochondrion. The mitochondrial glutathione reductase activity was strongly dependent on NADPH and not NADH.