Email this article Influence of dicarbonyls on kinetic characteristics of glutathione peroxidase
- Authors: Lankin V.Z.1, Shumaev K.B.1,2, Tikhaze A.K.1, Kurganov B.I.2
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Affiliations:
- Russian Cardiology Research and Production Center
- Bach Institute of Biochemistry, Federal Research Center “Fundamentals of Biotechnology”
- Issue: Vol 475, No 1 (2017)
- Pages: 287-290
- Section: Biochemistry, Biophysics, and Molecular Biology
- URL: https://journal-vniispk.ru/1607-6729/article/view/211960
- DOI: https://doi.org/10.1134/S1607672917040123
- ID: 211960
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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 Km and Vmax 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.
About the authors
V. Z. Lankin
Russian Cardiology Research and Production Center
Author for correspondence.
Email: lankin941@mail.ru
Russian Federation, Moscow, 121552
K. B. Shumaev
Russian Cardiology Research and Production Center; Bach Institute of Biochemistry, Federal Research Center “Fundamentals of Biotechnology”
Email: lankin941@mail.ru
Russian Federation, Moscow, 121552; Moscow, 119071
A. K. Tikhaze
Russian Cardiology Research and Production Center
Email: lankin941@mail.ru
Russian Federation, Moscow, 121552
B. I. Kurganov
Bach Institute of Biochemistry, Federal Research Center “Fundamentals of Biotechnology”
Email: lankin941@mail.ru
Russian Federation, Moscow, 119071
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