Gilevich S N, Gur'ev O L, Shkumatov V M, Chashchin V L, Akhrem A A
Biokhimiia. 1985 Aug;50(8):1342-9.
Hepatoredoxin purified to homogeneity from bovine liver mitochondria has been characterized for the first time in terms of its most important physico-chemical properties. The protein was found to contain in its active center a [2Fe-2S] cluster and has in the oxidized state an absorption maxima at 280, 320, 415 and 455 nm. The spectrophotometric index of purity, A415/A280 of the homogeneous native preparation is 0.84; extinction coefficient, epsilon 415, is 9800 M-1cm-1. The Mr of hepatoredoxin as evidenced by data from SDS gel electrophoresis is 12 500 Da; pI is 4.2. Hepatoredoxin is necessary for the reconstitution of the C27-steroid hydroxylase activity and can be substituted for by a related protein, adrenodoxin. All the above parameters as well as the circular dichroism spectra, immunochemical properties and sequence of the initial five N-terminal amino acids of hepatoredoxin and adrenodoxin are either coincident or very close. At the same time, the amino acid composition of these ferredoxins, apart from some common features, has individual peculiarities.
首次从牛肝线粒体中纯化出的均一肝铁氧还蛋白，已根据其最重要的物理化学性质进行了表征。发现该蛋白质的活性中心含有一个[2Fe-2S]簇，在氧化态下在280、320、415和455nm处有最大吸收峰。均一的天然制剂的分光光度纯度指数A415/A280为0.84；消光系数ε415为9800M-1cm-1。SDS凝胶电泳数据表明肝铁氧还蛋白的Mr为12500Da；等电点为4.2。肝铁氧还蛋白对于C27-类固醇羟化酶活性的重建是必需的，并且可以被一种相关蛋白质肾上腺铁氧还蛋白替代。肝铁氧还蛋白和肾上腺铁氧还蛋白的所有上述参数以及圆二色光谱、免疫化学性质和最初五个N端氨基酸的序列要么一致，要么非常接近。同时，这些铁氧还蛋白的氨基酸组成，除了一些共同特征外，还有各自的特点。
