Glutathionylation of the alpha-subunit of Na,K-ATPase from rat heart by oxidized glutathione inhibits the enzyme.
Biochemistry (Mosc)
; 79(2): 158-64, 2014 Feb.
Article
en En
| MEDLINE
| ID: mdl-24794731
ABSTRACT
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.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Procesamiento Proteico-Postraduccional
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ATPasa Intercambiadora de Sodio-Potasio
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Disulfuro de Glutatión
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Subunidades de Proteína
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Miocardio
Límite:
Animals
Idioma:
En
Revista:
Biochemistry (Mosc)
Año:
2014
Tipo del documento:
Article
País de afiliación:
Rusia