Abstract
Abstract The specificity of protein acceptors in the arginine transfer reaction has been investigated employing the criterion that a true acceptor be capable of accepting nearly stoichiometric quantities of arginine in the reaction catalyzed by arginyl-tRNA-protein transferase. A single protein was found to account for about 50% of the total acceptor activity in crude soluble extracts from rabbit liver. This protein was isolated and identified as rabbit albumin on the basis of its electrophoretic mobility, molecular weight, and amino acid composition. Of 38 defined proteins and polypeptides which have been tested, seven were found to function as acceptors. These were bovine, rabbit, and human albumins, bovine thyroglobulin, two human Bence-Jones proteins, and soybean trypsin inhibitor. These proteins are all known to have aspartic or glutamic acid as their NH2-terminal residue. The results indicate that the arginine-transfer reaction is highly specific with respect to protein acceptors and that this specificity is based on the presence of aspartic acid or glutamic acid at the NH2 termini.
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