Purification and characterization of lysyl-tRNA synthetase after dissociation of the particulate aminoacyl-tRNA synthetases from rat liver.
作者： D.L. Johnson , C. Van Dang , D.C. Yang
DOI: 10.1016/S0021-9258(19)85673-9
关键词:
摘要: The major aminoacyl-tRNA synthetase complex (the 24 S complex) isolated from rat liver, which contains lysyl-, leucyl-, and arginyl-tRNA activities, is dissociated into fully active free synthetases by column chromatography on diaminooctyl-Sepharose. During the hydrophobic interaction chromatography, more than a quantitative yield of lysyl-tRNA activity obtained. synthetase, complex, purified about 2,000-fold with 13% conventional chromatography. Lysyl-tRNA also affinity lysyl-diaminohexyl-Sepharose. Free as evidently dimeric enzyme subunit molecular weight 66,000 +/- 3,000, determined gel electrophoresis, sucrose gradient centrifugation filtration.
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