Enviar artigo por via de e-mail Influence of dicarbonyls on kinetic characteristics of glutathione peroxidase
- Autores: Lankin V.Z.1, Shumaev K.B.1,2, Tikhaze A.K.1, Kurganov B.I.2
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Afiliações:
- Russian Cardiology Research and Production Center
- Bach Institute of Biochemistry, Federal Research Center “Fundamentals of Biotechnology”
- Edição: Volume 475, Nº 1 (2017)
- Páginas: 287-290
- Seção: Biochemistry, Biophysics, and Molecular Biology
- URL: https://journals.rcsi.science/1607-6729/article/view/211960
- DOI: https://doi.org/10.1134/S1607672917040123
- ID: 211960
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Resumo
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.
Sobre autores
V. Lankin
Russian Cardiology Research and Production Center
Autor responsável pela correspondência
Email: lankin941@mail.ru
Rússia, Moscow, 121552
K. Shumaev
Russian Cardiology Research and Production Center; Bach Institute of Biochemistry, Federal Research Center “Fundamentals of Biotechnology”
Email: lankin941@mail.ru
Rússia, Moscow, 121552; Moscow, 119071
A. Tikhaze
Russian Cardiology Research and Production Center
Email: lankin941@mail.ru
Rússia, Moscow, 121552
B. Kurganov
Bach Institute of Biochemistry, Federal Research Center “Fundamentals of Biotechnology”
Email: lankin941@mail.ru
Rússia, Moscow, 119071
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