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Purification and characterization of lysyl-tRNA synthetase after dissociation of the particulate aminoacyl-tRNA synthetases from rat liver.

Authors: Johnson, DL  Van Dang, C  Yang, DC 
Citation: Johnson DL, etal., J Biol Chem. 1980 May 10;255(9):4362-6.
Pubmed: (View Article at PubMed) PMID:7372681

The major aminoacyl-tRNA synthetase complex (the 24 S complex) isolated from rat liver, which contains lysyl-, leucyl-, and arginyl-tRNA synthetase activities, is dissociated into fully active free aminoacyl-tRNA synthetases by column chromatography on diaminooctyl-Sepharose. During the hydrophobic interaction chromatography, more than a quantitative yield of the lysyl-tRNA synthetase activity is obtained. The free lysyl-tRNA synthetase, dissociated from the synthetase complex, is purified about 2,000-fold with a 13% yield by conventional column chromatography. Lysyl-tRNA synthetase is also purified from the 24 S synthetase complex by affinity column chromatography on lysyl-diaminohexyl-Sepharose. Free lysyl-tRNA synthetase as dissociated from the synthetase complex, is evidently a dimeric enzyme with a subunit molecular weight of 66,000 +/- 3,000, as determined by gel electrophoresis, sucrose gradient centrifugation and gel filtration.


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CRRD Object Information
CRRD ID: 2303393
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.