We studied the effect of Cl− (10–75 mM) and \documentclass[12pt]{minimal}
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\begin{document}$$ {\text{HCO}}_3^{-} $$\end{document} ions (10–25 mM) on the ATP-dependent GABAA receptor-coupled Cl− channel (Cl−-ATPase) in rat brain plasma membranes. The total enzyme activity was detected in the presence of both anions at a Cl−/\documentclass[12pt]{minimal}
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\begin{document}$$ {\text{HCO}}_3^{-} $$\end{document} ratio of 5:1 (Cl−, \documentclass[12pt]{minimal}
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\begin{document}$$ {\text{HCO}}_3^{-} $$\end{document}-ATPase). Specific inhibitors of P-type transport ATPases (N-ethylmaleimide, ovanadate, and oligomycin) suppressed Cl−, \documentclass[12pt]{minimal}
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\begin{document}$$ {\text{HCO}}_3^{-} $$\end{document}-ATPase, while the Cl−- and \documentclass[12pt]{minimal}
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\begin{document}$$ {\text{HCO}}_3^{-} $$\end{document}-ATPase activities were low sensitive to these ligands. Bicuculline abolished the activating effect of Cl− and \documentclass[12pt]{minimal}
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\begin{document}$$ {\text{HCO}}_3^{-} $$\end{document} ions on the enzyme. \documentclass[12pt]{minimal}
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\begin{document}$$ {\text{HCO}}_3^{-} $$\end{document} ions had no effect on the ATP-dependent Cl− transport into proteoliposomes (with the involvement of reconstituted ATPase). In experiment with Cl−-preloaded liposomes, addition of \documentclass[12pt]{minimal}
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\begin{document}$$ {\text{HCO}}_3^{-} $$\end{document} ions to the incubation medium caused the reversion of Cl− transport (ion efflux from liposomes). Our results suggest that \documentclass[12pt]{minimal}
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\begin{document}$$ {\text{HCO}}_3^{-} $$\end{document} ions play an important role in the modification of properties of the ATP-dependent GABAA receptor-coupled Cl− channel and GABAA receptor-induced Cl−/\documentclass[12pt]{minimal}
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\begin{document}$$ {\text{HCO}}_3^{-} $$\end{document} exchange. These ions are probably involved in GABAA receptor-induced Cl−/\documentclass[12pt]{minimal}
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\begin{document}$$ {\text{HCO}}_3^{-} $$\end{document} exchange in neuronal membranes.
