Abstract
The incorporation of arginine into hot trichloroacetic acid-insoluble material by a 150 000 · g supernatant fraction from sheep thyroid cytoplasm has been studied. 1. 1. Incorporated arginine contains a free α-amino group as judged by the fluorodinitrobenzene reaction. It can be recovered as free arginine after acid hydrolysis or digestion by pronase. 2. 2. Arginyl-tRNA is an intermediate and an enzyme has been partially purified which transfers arginine from tRNA to protein. This enzymatic transfer displays a partial requirement for a non-enzymatic protein. Boiled supernatant fraction, albumin and thyroglobulin fulfill this function, whereas hemoglobin, myoglobin, cytochrome c and polyaspartic acid do not. 3. 3. The transfer has a pH optimum between 9.0 and 9.8 and is highly dependent upon the presence of mercaptoethanol and upon the ionic strength of the reaction mixture. It does not require ribosomes, Mg 2+ nor GTP and it is neither inhibited by puromycin nor stimulated by poly(A, G). 4. 4. A similar system for the incorporation of arginine exists in the soluble fraction of rabbit liver cytoplasm. The data are most consistent with an addition reaction in which arginine is transferred from tRNA onto certain preexisting proteins.
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