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

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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.

FTICR allowed characterization of 4-hydroxy-2-nonenal (HNE)-modified apomyoglobin (an expanded spectrum of the +15 charge state is shown)

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Acknowledgment

This research has been supported by the grant AG025384 from the National Institutes of Health. Laszlo Prokai is the Robert A. Welch Professor at the University of North Texas Health Science Center.

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Authors and Affiliations

  1. Department of Molecular Biology & Immunology, University of North Texas Health, Science Center, 3500 Camp Bowie Boulevard, Fort Worth, TX, 76107-2699, USA

    Navin Rauniyar, Stanley M. Stevens Jr & Laszlo Prokai

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  1. Navin Rauniyar
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  2. Stanley M. Stevens Jr
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  3. Laszlo Prokai
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Correspondence to Laszlo Prokai.

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Rauniyar, N., Stevens, S.M. & Prokai, L. Fourier transform ion cyclotron resonance mass spectrometry of covalent adducts of proteins and 4-hydroxy-2-nonenal, a reactive end-product of lipid peroxidation. Anal Bioanal Chem 389, 1421–1428 (2007). https://doi.org/10.1007/s00216-007-1534-2

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  • DOI: https://doi.org/10.1007/s00216-007-1534-2

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