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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >A new selenoprotein from human lung adenocarcinoma cells: Purification, properties, and thioredoxin reductase activity
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A new selenoprotein from human lung adenocarcinoma cells: Purification, properties, and thioredoxin reductase activity

机译:来自人肺腺癌细胞的一种新型硒蛋白:纯化,性质和硫氧还蛋白还原酶活性

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摘要

We report the isolation and characterization of a new selenoprotein from a human lung adenocarcinoma cell line, NCI-H441. Cells were grown in RPMI 1640 medium containing 10/100 (vol/vol) fetal bovine serum and 0.1 μM [~75Se]selenite. A ~75Se-labeled protein was isolated from sonic extracts of the cells by chromatography on DE-23, phenyl- Sepharose, heparin-agarose, and butyl-Sepharose. The pro- tein, a homodimer of 57-kDa subunits, was shown to contain selenium in the form of selenocysteine; hydrolysis of the protein alkylated with either iodoacetate or 3-bromopropi- onate yielded Se-carboxymethyl-selenocysteine or Se-carboxyethyl- selenocysteine, respectively.
机译:我们报告了从人类肺腺癌细胞系NCI-H441分离和鉴定一种新的硒蛋白。细胞在含有10/100(vol / vol)胎牛血清和0.1μM[〜75Se]硒沸石的RPMI 1640培养基中生长。通过在DE-23,苯基-琼脂糖,肝素-琼脂糖和丁基-琼脂糖上层析,从细胞的声音提取物中分离出〜75Se标记的蛋白质。蛋白质,一种57kDa亚基的同型二聚体,被证明含有硒代半胱氨酸形式的硒。用碘乙酸盐或3-溴丙酸烷基化的蛋白质水解后分别生成Se-羧甲基-硒代半胱氨酸或Se-羧乙基-硒代半胱氨酸。

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