[The sensitivity of catalytic subunit isoforms of Na+,K+-ATPase of rat brain to peroxide membrane modification].
The comparative study of the sensitivity of Na+, K(+)-ATPase isozymes from cerebral cortex to ascorbate-dependent membrane peroxidation was conducted. With highly inactivated Na+, K(+)-ATPase the degree of inactivation of the SH-dependent ouabain-sensitive forms alpha+ (alpha 2 and alpha 3) is higher than glycoside-resistant isoform alpha 1. The process is accompanied by simultaneous lipid peroxidation and decrease of SH-groups amount in enzyme preparations. The combined nature of the oxidative Na+, K(+)-ATPase inactivation, accompanied by the direct oxidation of enzyme SH-groups and modification of lipid environment is supposed.
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O.V. Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv.
D000818:Animals; D020134:Catalytic Domain; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D015227:Lipid Peroxidation; D009474:Neurons / Q000187:drug effects* / Q000201:enzymology / Q000648:ultrastructure; D010042:Ouabain / Q000494:pharmacology; D020033:Protein Isoforms / Q000187:drug effects*; D051381:Rats; D000254:Sodium-Potassium-Exchanging ATPase / Q000187:drug effects*
D004791:Enzyme Inhibitors; D020033:Protein Isoforms; D010042:Ouabain; D000254:Sodium-Potassium-Exchanging ATPase
Chuvstvitel'nost' izoform kataliticheskoĭ sub"edinitsy Na+,K+-ATPazy mozga krysy k peroksidnoĭ modifikatsii membran.