Characteristic fragment ions associated with dansyl cadaverine and biotin cadaverine adducts on glutamine

Kevser Biberoglu, Lawrence M. Schopfer, Ozden Tacal, Oksana Lockridge

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Glutamine residues susceptible to transglutaminase-catalyzed crosslinking can be identified by incorporation of dansyl cadaverine or biotin cadaverine. Bacterial transglutaminase and human transglutaminase 2 were used to modify residues in beta-casein with dansyl cadaverine. Bacterial transglutaminase was used to modify residues in human butyrylcholinesterase with biotin cadaverine. Tryptic peptides were analyzed by LC-MS/MS on an Orbitrap Fusion Lumos mass spectrometer. Modified residues were identified in Protein Prospector searches of mass spectrometry data. The MS/MS spectra from modified casein included intense peaks at 336.2, 402.2, and 447.2 for fragments of dansyl cadaverine adducts on glutamine. The MS/MS spectra from modified butyrylcholinesterase included intense peaks at 329.2, 395.2, and 440.2 for fragments of biotin cadaverine adducts on glutamine. No evidence for transglutaminase-catalyzed adducts on glutamic acid, aspartic acid, or asparagine was found. Consistent with expectation, it was concluded that bacterial transglutaminase and human transglutaminase 2 specifically modify glutamine. The characteristic ions associated with dansyl cadaverine and biotin cadaverine adducts on glutamine are useful markers for modified peptides.

Original languageEnglish (US)
Article number113718
JournalAnalytical Biochemistry
Volume600
DOIs
StatePublished - Jul 1 2020

Keywords

  • Biotin cadaverine
  • Butyrylcholinesterase
  • Casein
  • Dansyl cadaverine
  • Mass spectrometry
  • Protein prospector
  • Transglutaminase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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