来自大鼠心脏的钠钾ATP酶α亚基被氧化型谷胱甘肽谷胱甘肽化会抑制该酶的活性。
Glutathionylation of the alpha-subunit of Na,K-ATPase from rat heart by oxidized glutathione inhibits the enzyme.
作者信息
Xianyu Meng, Petrushanko I Yu, Klimanova E A, Dergousova E A, Lopina O D
机构信息
Lomonosov Moscow State University, Department of Biochemistry, Biological Faculty, Moscow, 119991, Russia.
出版信息
Biochemistry (Mosc). 2014 Feb;79(2):158-64. doi: 10.1134/S0006297914020096.
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.
从大鼠心脏中提取的部分纯化的钠钾ATP酶制剂含有该酶的α1和α2亚型，结果显示这两个亚基均处于S-谷胱甘肽化状态。当制剂在二硫苏糖醇存在下分离时，α1亚基（而非α2亚基）的谷胱甘肽化被部分去除。加入氧化型谷胱甘肽会不可逆地抑制这两种亚型。含有α1亚基的酶的抑制呈双相性，抑制的速率常数分别为3745 ± 360和246 ± 18 M⁻¹·min⁻¹。ATP、ADP和AMP可保护钠钾ATP酶不被氧化型谷胱甘肽灭活。
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