Simultaneous purification and some properties of aspartate: tRNA ligase and seven other amino-acid:tRNA ligases from Escherichia coli.
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%. Aspartate: tRNA ligase, which has not been obtained in a highly purified form before, has been characterized in terms of its molecular parameters.
D001224:Aspartic Acid; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D011118:Polynucleotide Ligases / Q000302:isolation & purification*; D011130:RNA Ligase (ATP) / Q000302:isolation & purification* / Q000378:metabolism; D012343:RNA, Transfer; D013379:Substrate Specificity
D001224:Aspartic Acid; D012343:RNA, Transfer; D011118:Polynucleotide Ligases; D011130:RNA Ligase (ATP)