فهرست نشریات علمی دسترسی آزاد ایران

Glyoxalase 1 (Glo I), a crucial enzyme with multifaceted roles in various physiological and pathological processes, has garnered significant attention in recent years. As a critical detoxification enzyme, Glo I plays a vital role in neutralizing methylglyoxal (MG), a highly reactive and toxic dicarbonyl compound that can irreversibly modify proteins, lipids, and nucleic acids, leading to the formation of advanced glycation end-products (AGEs).The assay involves incubating the Glo I enzyme with glutathione and methylglyoxal, forming S-D-lactoylglutathione. This compound is then converted to lactic acid by adding sulfuric acid, which is oxidized to acetaldehyde using copper. Finally, acetaldehyde reacts with p-phenylphenol in sulfuric acid, creating a colored complex that absorbs light at 570 nm.The study also rigorously examines potential interferences from various biochemical substances, demonstrating the robustness of the proposed method. Experiments were conducted using different combinations of interfering biomolecules, including monosaccharides, amino acids, and proteins, to evaluate their impact on Glo I activity. The results indicate that the p-phenylphenol-Glo I method maintains its effectiveness in the presence of these substances.Furthermore, the method's accuracy was rigorously assessed through intra-day and inter-day analyses, with results expressed as percentage relative error (RE% < 0.4 %) to ensure precision in Glo I activity measurements. The current method exhibited excellent linearity across a broad range of 0.005–100 µM Lactate, with a high Pearson's correlation coefficient of 0.989. This work contributes valuable insights into the quantification of Glo I and holds significant implications for research in metabolic disorders and related fields.