Aspartyl Transfer Ribonucleic Acid Synthetase from Bakers' Yeast

Abstract

An aspartyl-tRNA synthetase has been purified from the genetic standard type yeast Saccharomyces cerevisiae S288C. Lysis with toluene was followed by six column chromatographic purification steps in the presence of glycerol. The enzyme was purified 166-fold with 12% recovery relative to activity in the initial chromatographic fraction. Significant activation occurred during chromatography on the cation exchange resin, Bio-Rex 70. The purified enzyme was free of other aminoacyl-tRNA synthetase activities tested except a trace of that for glutamyl-tRNA and was essentially pure by acrylamide gel electrophoresis.