Lindahl Marika, Florencio Francisco J
Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciónes Científicas, Universidad de Sevilla, Sevilla, Spain.
Proteomics. 2004 Feb;4(2):448-50. doi: 10.1002/pmic.200300604.
Redox signalling constitutes a topic within the field of cellular signal transduction which is attracting increasing interest. A major challenge is to identify the components of redox signalling pathways. Proteins containing cysteines that may reversibly form disulphides are principal candidates as transmitters of redox signals. Thioredoxins are small proteins containing a highly reactive dithiol. Here we present a simple procedure to isolate and separate proteins that contain redox active cysteines using a site-directed, histidine-tagged mutant of thioredoxin, which forms stable mixed disulphides with its targets.
氧化还原信号传导是细胞信号转导领域中一个越来越受关注的主题。一个主要挑战是确定氧化还原信号通路的组成部分。含有可可逆形成二硫键的半胱氨酸的蛋白质是氧化还原信号传递者的主要候选者。硫氧还蛋白是含有高活性二硫醇的小蛋白质。在这里，我们提出了一种简单的方法，使用硫氧还蛋白的定点、组氨酸标签突变体来分离和分离含有氧化还原活性半胱氨酸的蛋白质，该突变体与其靶标形成稳定的混合二硫键。
