Abstract

The incorporation of l-[U- 14C]leucine and l-[ring-2- U14C]histidine into the protein of a post-mitochondrial supernatant fraction from mouse liver is inhibited by salicylate concentrations of 1 mM and above. The intraperitoneal injection of 500–600 mg/kg of salicylate in the mouse causes the following: an increase in the liver concentration of leucine but not that of histidine; a decrease in the incorporation of radioactive leucine and histidine into liver protein in vitro; an inhibition of the incorporation of radioactivity from intraperitoneally injected leucine into liver protein in vivo; a decrease in the transfer of α-aminoisobutyrate from the peritoneum to the blood but not from the circulation to the tissues and an inhibition of protein biosynthesis in the liver after the intravenous administration of radioactive leucine and histidine. It is concluded that salicylate interferes with protein synthesis in mouse liver both in vitro and in vivo.

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