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  • Title: Physical and biochemical characterization of a purified arginyl-tRNA synthetase-lysyl-tRNA-synthetase complex from rat liver.
    Author: Van Dang C, Glinski RL, Gainey PC, Hilderman RH.
    Journal: Biochemistry; 1982 Apr 13; 21(8):1959-66. PubMed ID: 7082655.
    Abstract:
    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.
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