title: Fourier transform ion cyclotron resonance mass spectrometry of covalent adducts of proteins and 4-hydroxy-2-nonenal, a reactive end-product of lipid peroxidation.
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.
authors.affiliation: Department of Molecular Biology & Immunology, University of North Texas Health, Science Center, 3500 Camp Bowie Boulevard, Fort Worth, TX 76107-2699, USA.
authors.forename: Navin
authors.initials: N
authors.lastname: Rauniyar
authors.forename: Stanley M
authors.initials: SM
authors.lastname: Stevens
authors.forename: Laszlo
authors.initials: L
authors.lastname: Prokai
mesh_terms: D000447:Aldehydes / Q000032:analysis* / Q000737:chemistry; D017357:Cyclotrons; D005583:Fourier Analysis; D007328:Insulin / Q000032:analysis; D015227:Lipid Peroxidation; D011506:Proteins / Q000032:analysis* / Q000737:chemistry; D053719:Tandem Mass Spectrometry / Q000379:methods*