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- W2022721903 abstract "The nature and the role of eIF-2 phosphoprotein phosphatase in rabbit reticulocyte lysates have been examined. The eIF-2 phosphoprotein phosphatase is inhibited by a variety of divalent metal ions (Cd++>Ag++> Cu++>Pb++>Zn++>Co++>Sr++>Mo++) in lysates in situ. In addition, PPi, EDTA and NaF inhibit this enzyme. The eIF-2 phosphoprotein phosphatase is also inhibited by NaHSO3 and Na2S2O5. Na2S2O5 is, however, more effective. Na2S2O5 has been found to be a potent inhibitor of protein synthesis in lysates. This inhibition is associated with the phosphorylation of the 38,000-dalton subunit of initiation factor eIF-2. eIF-2 overcomes this inhibition. These findings suggest that under optimum conditions of protein synthesis the phosphorylation and dephosphorylation of eIF-2 are in a dynamic state of equilibrium in which dephosphorylation is favored. The inhibition of eIF-2 phosphoprotein phosphatase by Na2S2O5 shifts this equilibrium in favor of eIF-2 phosphorylation, consequently, protein synthesis is inhibited. The sulfhydryl nature of eIF-2 phosphoprotein phosphatase has been established." @default.
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- W2022721903 date "1981-09-01" @default.
- W2022721903 modified "2023-10-17" @default.
- W2022721903 title "Regulation of protein synthesis in rabbit reticulocyte lysates: Inhibition of eIF-2 phosphoprotein phosphatase by NaF, pyrophosphate and cations" @default.
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- W2022721903 doi "https://doi.org/10.1016/0006-291x(81)91484-4" @default.
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