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Updated: Feb 23, 2026

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
Published on: October 10, 2020
Influence of dicarbonyls on kinetic characteristics of glutathione peroxidase
V Z Lankin1, K B Shumaev2,3, A K Tikhaze2
1Russian Cardiology Research and Production Center, Ministry of Healthcare of the Russian Federation, Moscow, 121552, Russia. lankin941@mail.ru.
Abstract:
Se-containing glutathione peroxidase (GSH-Px) is one of the key enzymes of the body's antioxidant system. The kinetic characteristics of GSH-Px (substrate is tert-butyl hydroperoxide) after modification of the enzyme by various concentrations of natural dicarbonyls (glyoxal, methylglyoxal, malonic dialdehyde) were studied. It was shown that dicarbonyls affected both K m and V max for GSH-Px. It is suggested that the effect of various dicarbonyls on GSH-Px depends on the molecular mechanisms of their interaction with the amino acid residues of the enzyme.
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