Physical and biochemical characterization of a purified arginyl-tRNA synthetase-lysyl-tRNA-synthetase complex from rat liver.
Arginyl- and lysyl-tRNA synthetases copurify throughout a six-step chromatographic procedure resulting in a purification of 605- and 559-fold, respectively. The purified enzymes were estimated to be 98% pure with a stoichiometry of 1:1 from acrylamide gel electrophoresis under denaturing conditions. On the basis of a native molecular weight of 285000 calculated from s20,w, Rs, and V and subunit molecular weights of 73000 and 65000 obtained by sodium dodecyl sulfate gel electrophoresis, the synthetases appear to exist as a tetramer. The tetrameric structure was also supported by cross-linking studies. These results are consistent with an alpha 2 beta 2 structure, but an alpha beta structure has not been ruled out.
D000604:Amino Acyl-tRNA Synthetases / Q000302:isolation & purification*; D000818:Animals; D001126:Arginine-tRNA Ligase / Q000302:isolation & purification*; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D007525:Isoelectric Focusing; D008099:Liver / Q000201:enzymology*; D008250:Lysine-tRNA Ligase / Q000302:isolation & purification*; D046911:Macromolecular Substances; D008970:Molecular Weight; D051381:Rats
D046911:Macromolecular Substances; D000604:Amino Acyl-tRNA Synthetases; D001126:Arginine-tRNA Ligase; D008250:Lysine-tRNA Ligase