Fourier transform ion cyclotron resonance mass spectrometry of covalent adducts of proteins and 4-hydroxy-2-nonenal, a reactive end-product of lipid peroxidation

Navin Rauniyar, Stanley M. Stevens, Laszlo Prokai

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

Covalent adduction of the model protein apomyoglobin by 4-hydroxy-2-nonenal, a reactive end-product of lipid peroxidation, was characterized by nanoelectrospray ionization Fourier transform ion cyclotron resonance mass spectrometry (FTICR). The high mass resolving power and mass measurement accuracy of the instrument facilitated a detailed compositional analysis of the complex reaction product without the need for deconvolution and transformation to clearly show the pattern of adduction and component molecular weights. Our study has also demonstrated the value of electron capture dissociation over collision-induced dissociation for the tandem mass spectrometric determination of site modification for the 4-hydroxy-2-nonenal adduct of oxidized insulin B chain as an example. [Figure not available: see fulltext.]

Original languageEnglish
Pages (from-to)1421-1428
Number of pages8
JournalAnalytical and Bioanalytical Chemistry
Volume389
Issue number5
DOIs
StatePublished - 1 Nov 2007

Keywords

  • 4-Hydroxy-2-nonenal
  • Electron capture dissociation
  • Electrospray ionization
  • Fourier transform ion cyclotron resonance mass spectrometry
  • Protein carbonylation

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