Simultaneous Purification and Some Properties of Aspartate: tRNA Ligase and Seven Other Amino-acid: tRNA Ligases from Escherichia coli

Abstract

A procedure is described for the purification of the aspartate: tRNA ligase from Escherichia coli to a stage where it was homogeneous by polyacrylamide gel electrophoresis. From the same batch of E. coli the lysine, phenylalanine and serine ligases were obtained in an apparently homogeneous form while the alanine, glutamine, leucine and valine enzymes had a purity varying from 20% to 80 %.

Readinbg of the lysine codons in the MS 2 coat protein cistron during protein synthesis in vitro

“…Lysine:tRNA ligase from E. coli was purified to homogeneity as in [6,7]. The enzyme was dissolved in 0.5 ml 0.05 M K-phosphate buffer (pH 7.5) to give 1 mg enzyme/ml final cont.…”