Abstract
A protein fraction (Fraction X) was isolated from rat liver cell sap from which ribosomes had been removed previously by centrifugation for 14.5—15 h at 105000×g. Fraction X sedimented at approx. 28 S. The isolated fraction restored amino acid incorporation into protein in vitro to values obtained when total cell sap was used as an enzyme source. The active fraction was purified by precipitation with ammonium sulphate and by gel filtration on Sephadex G-200. This purification resulted in removal of the ribonuclease inhibitor which was present in the crude Fraction X. The result of each purification step was examined by electrophoresis on polyacrylamide gels. Evidence is provided that the activity of fraction X cannot be ascribed to ribosomal subunits, but is mainly due to the action of synthetases.
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