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谷胱甘肽过氧化物酶能够催化H₂O₂氧化还原型谷胱甘肽(GSH),生成氧化型谷胱甘肽(GSSG)。GSSG在谷胱甘肽还原酶(GR)的作用下,与NADPH反应重新生成GSH。GPX4抑制剂通过抑制GPX4活性,从而降低NADPH的消耗速率。NADPH在340 nm处具有特征吸收峰,通过测定该波长下吸光度下降的速率,即可定量表征谷胱甘肽过氧化物酶4的活性。
Glutathione peroxidase 4 (GPX4) catalyzes the oxidation of reduced glutathione (GSH) by H₂O₂ to generate oxidized glutathione (GSSG). GSSG is then recycled to GSH by glutathione reductase (GR) in the presence of NADPH. GPX4 inhibitors suppress GPX4 activity, thereby reducing the rate of NADPH consumption. NADPH exhibits a characteristic absorbance peak at 340 nm. By measuring the rate of decrease in absorbance at this wavelength, the activity of glutathione peroxidase 4 can be quantitatively determined.