Abstract
Abstract The presence of arginyl-tRNA protein transferase has been shown in a variety of mammalian cells in culture. Analysis by sodium dodecyl sulfate acrylamide gel electrophoresis of the available endogenous acceptor proteins (proteins that can be arginylated at their amino terminus by this enzyme) reveals that there are at least two such proteins (designated Peaks I and II) with the same relative migration during electrophoresis in a variety of tissues. Analysis of baby hamster kidney cells (BHK), polyoma-transformed BHK, and herpes simplex-infected BHK showed Peak II, but in the general region of Peak I there were two peaks. Other peaks, which varied in migration and appearance, were also observed in the various cell preparations. The incorporation of labeled arginine was inhibited by ribonuclease, canavanine, hemoglobin, and hemin but not by puromycin nor cycloheximide. The specificity of the enzyme from different species for exogenous acceptor proteins of various species is reported.
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