مشخصات پژوهش

Glutathione peroxidase (GPx) is an important enzyme in the cellular antioxidant defense system. It plays a vital role in protecting cells from oxidative damage caused by reactive oxygen species, such as hydrogen peroxide (H2O2). Accurately measuring GPx activity is essential for understanding its role in various physiological and pathological conditions, including its potential as a biomarker for oxidative stress-related diseases. However, current methods for measuring GPx activity have limitations, including low sensitivity, reliance on expensive reagents, and susceptibility to interference from other cellular components [1]. The problem statement underscores the challenges of measuring glutathione peroxidase (GPx) activity due to the complexity of existing protocols. Current methods, such as those developed by Flohé and Günzler, require strong acids to stop the GPx reaction, which can be hazardous and impractical. Additionally, the GPx-DTNB method, which utilizes Ellman's reagent for colorimetric assessment of glutathione (GSH) consumption, has drawbacks, such as the need for protein precipitation and difficulties in implementation with a microplate reader [2]. These limitations contribute to the insensitivity of the GPx-DTNB assay when compared to alternative protocols. The present study aims to overcome these limitations by developing a new, more efficient method for assessing GPx activity, which eliminates the need for concentrated acids and is suitable for both cuvette and microplate applications [3].