期刊
BIOCHEMISTRY-MOSCOW
卷 79, 期 2, 页码 158-164出版社
MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1134/S0006297914020096
关键词
Na; K-ATPase; glutathionylation; oxidized glutathione; rat heart
资金
- Russian Foundation for Basic Research [12-04-00403-a, 14-04-01737-A]
- Russian Academy of Sciences Presidium
- Russian Federation Ministry of Education and Science program [16.512.11.2280]
A partially purified Na,K-ATPase preparation from rat heart containing alpha 1- and alpha 2-isoforms of the enzyme was shown to include both subunits in S-glutathionylated state. Glutathionylation of the alpha 1-subunit (but not of the alpha 2-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 alpha 1-subunit was biphasic, and the rate constants of the inhibition were 3745 +/- 360 and 246 +/- 18 M-1 center dot min(-1). ATP, ADP, and AMP protected the Na,K-ATPase against inactivation by oxidized glutathione.
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