Affinity chromatography of rat liver aminoacyl-tRNA synthetase complex |
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| Authors: | C V Dang D C Yang |
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| Affiliation: | Department of Chemistry, Georgetown University Washington, D.C. 20057 USA |
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| Abstract: | The affinity column lysyldiaminohexyl-Sepharose 4B has been synthesized for the purification of aminoacyl-tRNA synthetase complexes. Lysyl-tRNA synthetase (EC 6.1.1.6) bound specifically to the Sepharose-bound lysine. The purified lysyl-tRNA synthetase was associated with arginyl-tRNA synthetase (EC 6.1.1.16) and sedimented at 18S and 12S. A 24S lysyl-tRNA synthetase bound specifically to the affinity column and also found associated with arginyl-tRNA synthetase. The results favor the model of a heterotypic multienzyme complex of mammalian aminoacyl-tRNA synthetases. |
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