Glutathionylation of the alpha-subunit of Na,K-ATPase from rat heart by oxidized glutathione inhibits the enzyme
| Autor: | Olga D. Lopina, E. A. Dergousova, I. Yu. Petrushanko, Meng Xianyu, E. A. Klimanova |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
chemistry.chemical_classification
GPX3 Glutathione Disulfide Sodium-Potassium-Exchanging ATPase Protein subunit Myocardium General Medicine Biochemistry Molecular biology Dithiothreitol Rats chemistry.chemical_compound Protein Subunits Enzyme chemistry Glutathione disulfide Animals Na+/K+-ATPase Enzyme Inhibitors Rats Wistar Protein Processing Post-Translational G alpha subunit |
| Zdroj: | Biochemistry. Biokhimiia. 79(2) |
| ISSN: | 1608-3040 |
| Popis: | A partially purified Na,K-ATPase preparation from rat heart containing α1- and α2-isoforms of the enzyme was shown to include both subunits in S-glutathionylated state. Glutathionylation of the α1-subunit (but not of the α2-subunit) was partially removed when the preparation was isolated in the presence of dithiothreitol. The addition of oxidized glutathione irreversibly inhibited both isoforms. Inhibition of the enzyme containing the α1-subunit was biphasic, and the rate constants of the inhibition were 3745 ± 360 and 246 ± 18 M(-1)·min(-1). ATP, ADP, and AMP protected the Na,K-ATPase against inactivation by oxidized glutathione. |
| Databáze: | OpenAIRE |
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