<Originals>The Effect of Chlorpromazine on the Phosphorylation of Na^+, K^+-ATPase Preparation from Brain Microsomes
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The effect of chlorpromazine on the phosphorylation of the Na^+, K^+-ATPase preparation from guinea pig brain microsome was investigated. The membrane preparation showed two kinds of phosphorylation. One was Na^+-stimulated and unstable phosphorylation and the other was Mg^<2+>-dependent stable one. 1. Na^+-stimulated unstable phosphorylation was inhibited by higher concentrations of chlorpromazine. Ki of the drug on the Na^+-dependent phosphorylation was estimated at 2.5×10^<-4> M. This concentration was quite similar to the Ki on Na^+, K^+-ATPase activity and K^+-dependent phosphatase activity. It may be concluded from these results that the inhibition of chlorpromazine on Na^+, K^+-ATPase activity was produced by universal inhibition on the phosphorylation and dephosphorylation steps of the enzyme reaction. 2. Mg^<2+>-dependent stable phosphorylation was stimulated by lower concentrations of chlorpromazine. The stimulation occurred between 5×10^<-5> and 5×10^<-3> of chlorpromazine. Optimal stimulation was obtained by 2.5×10^<-4> M of chlorpromazine. The stimulation required Mg^<2+> and was inhibited by EDTA. Ouabain and K^+ did not affect the stimulation. NaI treatment of the microsomal preparation increased the stimulation comparing with the crude preparation. Then it was suggested that the chlorpromazine stimulation of the membrane phosphorylation may be related to the Mg^<2+>-ATPase activity of the Na^+, K^+-ATPase system and the membrane stabilizing or protective action of chlorpromazine.
- 近畿大学の論文
- 1979-06-28
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