TrxR是一种NADPH依赖的包含FAD结构域的二聚体硒酶，属于吡啶核苷酸-二硫化物氧化还原酶家族成员，与硫氧还蛋白以及NADPH共同构成了硫氧还蛋白系统。TrxR与GR活性类似，催化GSSG还原生成GSH，是谷胱甘肽氧化还原循环关键酶之一。 测定原理：TrxR催化NADPH还原DTNB生成TNB和NADP⁺，TNB在412 nm有特征吸收峰，通过测定412nm波长处TNB的增加速率，即可计算TrxR活性。
Thioredoxin reductase (TrxR) is a NADPH-dependent dimeric selenoenzyme containing an FAD domain, belonging to the pyridine nucleotide-disulfide oxidoreductase family. Together with thioredoxin and NADPH, it constitutes the thioredoxin system. TrxR activity is analogous to that of glutathione reductase (GR), catalyzing the reduction of oxidized glutathione (GSSG) to reduced glutathione (GSH), making it a key enzyme in the glutathione redox cycle. Assay Principle: TrxR catalyzes the NADPH-dependent reduction of 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) to produce 5-thio-2-nitrobenzoic acid (TNB) and NADP⁺. TNB exhibits a characteristic absorption peak at 412 nm. The activity of TrxR is calculated by measuring the rate of increase in TNB at 412 nm.
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