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Physical and biochemical characterization of a purified arginyl-tRNA synthetase-lysyl-tRNA-synthetase complex from rat liver.

Authors: Van Dang, C  Glinski, RL  Gainey, PC  Hilderman, RH 
Citation: Van Dang C, etal., Biochemistry. 1982 Apr 13;21(8):1959-66.
Pubmed: (View Article at PubMed) PMID:7082655

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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RGD Object Information
RGD ID: 2303394
Created: 2009-02-11
Species: All species
Last Modified: 2009-02-11
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.