Glutathionylation of the Alpha-Subunit of Na,K-ATPase from Rat Heart by Oxidized Glutathione Inhibits the Enzyme

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Meng Xianyu¹, I. Yu. Petrushanko², E. A. Klimanova¹, E. A. Dergousova¹, and O. D. Lopina^1*

¹Lomonosov Moscow State University, Department of Biochemistry, Biological Faculty, 119991 Moscow, Russia; fax: (495) 939-3955; E-mail: od_lopina@mail.ru

²Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, ul. Vavilova 32, 119999 Moscow, Russia

^* To whom correspondence should be addressed.

Received November 1, 2013; Revision received November 21, 2013

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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.

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KEY WORDS: Na,K-ATPase, glutathionylation, oxidized glutathione, rat heart

DOI: 10.1134/S0006297914020096

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