Abstract
ADMINISTRATION of adrenocorticotrophin in vivo increases the incorporation of 14C-glycine into protein by the supernatant of adrenal homogenates centrifuged at 15,000g1. A factor of the soluble cell fraction (105,000g supernatant) has been shown to be rate limiting for in vitro protein synthesis and its activity is doubled by ACTH administration in rats. This factor was reported to be proteinaceous; its elution pattern from DEAE-cellulose columns2 was identical with liver aminoacyltransferase3. The increased activity of the microsomal fraction by treatment with ACTH was reported to be delayed compared with the soluble cell fraction4. Thus it was of interest to find whether polysomes, which are polymeres of ribosomes and messenger-RNA5,6, or the protein from the soluble adrenal cell fraction were rate limiting for protein synthesis.
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SCRIBA, P., FRIES, M. Aminoacyltransferase Stimulation of Protein Synthesis by Pig Adrenal Polysomes. Nature 214, 91–92 (1967). https://doi.org/10.1038/214091a0
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DOI: https://doi.org/10.1038/214091a0
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