Structure elucidation of DNA-protein crosslinks by using reductive desulfurization and liquid chromatography-tandem mass spectrometry

Susith Wickramaratne, Natalia Y. Tretyakova

Research output: Contribution to journalArticle

Abstract

Easier with ethyl: Guengerich and co-workers have developed a powerful new approach to the structure elucidation of hydrolytically stable AGT-DNA crosslinks by reductive desulfurization of the thioether linkage between AGT and DNA to convert cysteine DPCs to the corresponding ethyl-DNA adducts, which can be readily characterized by LC-MSn.

Original languageEnglish (US)
Pages (from-to)353-355
Number of pages3
JournalChemBioChem
Volume15
Issue number3
DOIs
StatePublished - Feb 10 2014

Keywords

  • DNA-protein crosslinks
  • O-alkylguanine DNA alkyltransferase
  • desulfurization
  • labile and nonlabile DNA adducts
  • liquid chromatography-tandem mass spectrometry

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