Thiol-Redox Proteomics to Study Reversible Protein Thiol Oxidations in Bacteria.
Thiol-Redox Proteomics to Study Reversible Protein Thiol Oxidations in Bacteria.
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DOI：
10.1007/978-1-4939-8695-8_18
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发表时间：
2018
影响因子：
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通讯作者：
Martina Rossius;Falko Hochgräfe;H. Antelmann
中科院分区：
文献类型：
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作者：
Martina Rossius;Falko Hochgräfe;H. Antelmann
巯基-氧化还原蛋白质组学方法是氧化还原生物学中迅速发展的工具。这些应用于鉴定和定量具有可逆硫醇氧化的蛋白质，这些蛋白质在细胞内正常生长和氧化应激条件下形成。具有可逆硫醇氧化的蛋白质通常通过还原硫醇的烷基化，随后二硫键的还原，接着新释放的硫醇的第二差异烷基化来制备。在这里，我们描述了两种方法，用于检测蛋白S-巯基化革兰氏阳性菌使用直接鸟枪法和荧光标记巯基氧化还原蛋白质组学方法，已成功地应用于我们以前的工作。
Thiol-redox proteomics methods are rapidly developing tools in redox biology. These are applied to identify and quantify proteins with reversible thiol oxidations that are formed under normal growth and oxidative stress conditions inside cells. The proteins with reversible thiol oxidations are usually prepared by alkylation of reduced thiols, subsequent reduction of disulfide bonds followed by a second differential alkylation of newly released thiols. Here, we describe two methods for detection of proteinS-thiolations in Gram-positive bacteria using the direct shotgun approach and the fluorescent-label thiol-redox proteomics method that have been successfully applied in our previous work.