Studies on the protein synthesis in poisoning. III. Labeling of pH-5 enzyme with C14-glycine and the inhibition by para chloromercuribenzoate

The labeling of C14-glycine to pH-5 enzyme, PP32-ATP exchange by pH-5 enzyme, and the inhibitory action of p-chloromercuribenwate were examined. 1) The labeling of C14-glycine to pH-5 enzyme is inhibited by 10-4 mole of PCMB, and this inhibitory effect is reduced by addition of cysteine having 20 mole equivalent of PCMB. 2) The PP32-ATP exchange reaction is also reduced by addition of PCMB and inhibitory effect of PCMB is reduced by the addition of cysteine having 20 mole equivalent of PCMB. 3) These results show that the inhibition of the organic mercury compounds on the protein synthesis is responsible for attack the SH enzyme which catalyzes some amino-acid activation, and consequently influences activated amino-acid transfer reaction. 4) Paper electrophoretic pattern of pH-5 enzyme shows numerous peaks, each having the mobility between α2-globulin and γ-globulin.