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- W25535467 abstract "Eosinophil peroxidase (EPO) and myeloperoxidase (MPO) have been implicated in generating reactive species and promoting oxidative modifications in numerous diseases. The detection and identification of potential pathways has been proven extremely challenge due to evanescence nature of these reactive species. An alternative approach to study the involvement of oxidative modification is to detect and quantify the stable molecular fingerprints, like oxidized tyrosine species, in biological matrices. Previously reported analytical methods for quantifying oxidized amino acids have typically been limited by: low sensitivity, specificity and the failure of detection potential oxidation products generated during sample handling. Using GC/MS in combination with stable isotope dilution, a sensitive and self-quality control assay was developed. Using this isotope-dilution GC/MS and multiple allergen challenge models, we demonstrate that EPO is the major pathway for generating protein-bound 3-bromotyrosine in vivo. However, the need for chemical derivatization of samples increases the possibility that artifactual generation of oxidation products which may interfere with the detection of native levels. Requirement of unique derivatization reagent for each oxidized tyrosine results sample analysis both cumbersome and time/labor intensive. Therefore, we develop a liquid chromatography with on-line electrospray ionization tandem mass" @default.
- W25535467 created "2016-06-24" @default.
- W25535467 creator A5009892379 @default.
- W25535467 date "2008-01-01" @default.
- W25535467 modified "2023-09-24" @default.
- W25535467 title "Mass spectrometry-based high throughput approach for identification of molecular modification of oxidative process in respiratory diseases." @default.
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