Abstract
Abstract The arginyl transfer ribonucleic acid-protein transferase has been purified nearly 7000-fold from the supernatant fraction of rabbit liver cytoplasm by a procedure including ammonium sulfate fractionation, precipitation at pH 5.2, chromatography on carboxymethyl cellulose, and chromatography on diethylaminoethyl cellulose. The purified preparations show one major and two minor components in polyacrylamide disc gel electrophoresis and 1 mg of protein catalyzes the transfer at 37° of approximately 135 nmoles of arginine per min from tRNA to the amino-terminal aspartic acid residue of bovine serum albumin. Arginine can be quantitatively transferred from tRNA to protein and is the only amino acid which participates in this reaction. A sulfhydryl compound is required and maximal rates are obtained at pH 9 with 0.1 m 2-mercaptoethanol or 10 mm dithiothreitol. There is also a requirement for a monovalent cation with an optimal reaction occurring at 0.2 m KCl. Transfer is completely dependent upon the presence of a suitable acceptor protein. When bovine serum albumin is used in limiting amounts, 1 molecule of arginine is transferred from tRNA for each molecule of albumin. Bovine thyroglobulin appears to accept 2 molecules of arginine per molecule. Under similar conditions other proteins were far less effective as acceptors.
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