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

D. L. Johnson, C. Van Dang, D. C. Yang

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)4362-4366
Number of pages5
JournalJournal of Biological Chemistry
Volume255
Issue number9
StatePublished - May 10 1980
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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