Glutathionylation of the alpha-subunit of Na,K-ATPase from rat heart by oxidized glutathione inhibits the enzyme
Glutathionylation of the alpha-subunit of Na,K-ATPase from rat heart by oxidized glutathione inhibits the enzyme
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DOI：
10.1134/s0006297914020096
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发表时间：
2014-02-01
影响因子：
2.8
通讯作者：
Lopina, O. D.
中科院分区：
文献类型：
--
作者：
Meng Xianyu;Petrushanko, I. Yu;Lopina, O. D.
一个部分纯化的钠，钾-ATP酶制剂从大鼠心脏含有α 1-和α 2-异构体的酶被证明包括两个亚基的S-谷胱甘肽状态。当在二硫苏糖醇存在下分离制备物时，α 1-亚基（但不包括α 2-亚基）的谷胱甘肽化被部分去除。氧化型谷胱甘肽的加入不可逆地抑制这两种亚型。含有α 1亚基的酶的抑制是双相的，抑制的速率常数为3745 +/- 360和246 +/- 18 M-1中心点min（-1）。ATP、ADP和AMP保护Na，K-ATP酶不被氧化型谷胱甘肽失活。
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.