PURIFICATION AND PROPERTIES OF RAT LUNG SOLUBLE GLUTATHIONE PEROXIDASE
PURIFICATION AND PROPERTIES OF RAT LUNG SOLUBLE GLUTATHIONE PEROXIDASE
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DOI：
10.1016/0005-2744(76)90110-8
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发表时间：
1976-01-01
期刊：
影响因子：
--
通讯作者：
TAPPEL, AL
中科院分区：
文献类型：
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作者：
CHIU, DTY;STULTS, FH;TAPPEL, AL
纯化谷胱甘肽周期氧化酶（谷胱甘肽：过氧化氢氧化还原酶，EC 1.11.1.9）。从大鼠肺可溶性部分提取2700倍。经十二烷基硫酸钠/尿素聚丙烯酰胺凝胶电泳，纯化酶均相。75Se示踪剂与酶活性共色谱，表明大鼠肺可溶性谷胱甘肽过氧化物酶是一种Se酶。该酶的分子量约为80,000 MW，含有4个相同的亚基。该酶的最佳活性为pH 8.8 ~ 9.1。该酶对氢过氧化物具有一般特异性，对还原性谷胱甘肽具有高特异性。纯化的肺可溶性谷胱甘肽过氧化物酶的动力学行为遵循乒乓机制：酶首先将脂质过氧化氢底物还原为相应的羟基脂肪酸，然后通过还原性谷胱甘肽再生为天然形式。
Gluthathione perioxidase (gluthatione:hydrogen-peroxide oxidoreductase, EC 1.11.1.9) was purified .apprx. 2700-fold from rat lung soluble fraction. The purified enzyme was homogeneous during sodium dodecyl sulfate/urea polyacrylamide gel electrophoresis. 75Se tracer cochromatographed with the enzyme activity, indicating that rat lung soluble gluthathione peroxidase is a Se enzyme. The enzyme had an approximate MW of 80,000 and contained 4 identical subunits. The optimal activity of the enzyme was between pH 8.8 and 9.1. The enzyme had general specificity toward hydroperoxides, and high specificity for reduced glutathione. The kinetic behavior of the purified lung soluble glutathione peroxidase followed a ping-pong-like mechanism: the enzyme 1st reduced the lipid hydroperoxide substrate to the corresponding hydroxy fatty acid, then was regenerated to the native form by reduced glutathione.