Affinity chromatography of rat liver aminoacyl-tRNA synthetase complex

Chi Van Dang, David C H Yang

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)709-714
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume80
Issue number4
DOIs
StatePublished - Feb 28 1978
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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