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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Definition of the mitochondrial proteome by measurement of molecular masses of membrane proteins
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Definition of the mitochondrial proteome by measurement of molecular masses of membrane proteins

机译：通过测量膜蛋白的分子质量来定义线粒体蛋白质组

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摘要

The covalent structure of a protein is incompletely defined by its gene sequence, and mass spectrometric analysis of the intact protein is needed to detect the presence of any posttranslational modifications. Because most membrane proteins are purified in detergents that are incompatible with mass spectrometric ionization techniques, this essential measurement has not been made on many hydrophobic proteins, and so proteomic data are incomplete. We have extracted membrane proteins from bovine mitochondria and detergent-purified NADH:ubiquinone oxidoreductase (complex 1) with organic solvents, fractionated the mixtures by hydrophilic interaction chromatography, and measured the molecular masses of the intact membrane proteins, including those of six subunits of complex I that are encoded in mitochondrial DNA. These measurements resolve long-standing uncertainties about the interpretation of the mitochondrial genoe, and they contribute significantly to the definition of the covalent composition of complex I.
机译：蛋白质的共价结构不能完全由其基因序列定义，因此需要对完整蛋白质进行质谱分析以检测任何翻译后修饰的存在。由于大多数膜蛋白是在与质谱电离技术不兼容的去污剂中纯化的，因此尚未对许多疏水蛋白进行必要的测量，因此蛋白质组学数据不完整。我们从牛线粒体中提取膜蛋白，并用有机溶剂从去污剂纯化的NADH：泛醌氧化还原酶（配合物1）中提取膜蛋白，通过亲水相互作用色谱法分离混合物，并测量完整膜蛋白的分子量，包括复合物的六个亚基的分子量。线粒体DNA中编码的I。这些测量解决了关于线粒体基因组解释的长期不确定性，并且它们对复合物I的共价组成的定义做出了重要贡献。

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