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[Effect of the protonophore carbonylcyanide-m-chlorophenylhydrazone on the localization of secreted alkaline phosphatase in E. coli].

It was shown that the total amount of synthesized alkaline phosphatase as well as the value of enzymatic activity in E. coli cells decrease in the presence of the protonophore, carbonylcyanide-m-chlorophenylhydrazone. The enzyme content in the periplasm also decreases, while the amount of the enzyme bound to the spheroplasts increases. This effect is enhanced with a rise in the protonophore concentration. An electron cytochemical analysis showed that in the presence of the protonophore, alkaline phosphatase is partly localized in the cytoplasm and on the inner surface of the cytoplasmic membrane, which is unobserved in control cells. It was assumed that carbonylcyanide-m-chlorophenylhydrazone suppresses the translocation of alkaline phosphatase across the cytoplasmic membrane and enzyme biosynthesis, on the whole.