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- W2094576754 endingPage "4627" @default.
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- W2094576754 abstract "Protein modifications, including oxidative modifications, glycosylations, and oxidized lipid–protein adducts, are becoming increasingly important as biomarkers and in understanding disease etiology. There has been a great deal of interest in mapping these on Apo B100 from low density lipoprotein (LDL). We have used extracted ion chromatograms of product ions generated using a very narrow mass window from high-resolution tandem mass spectrometric data collected on a rapid scanning quadrupole time-of-flight (QTOF) instrument, to selectively and sensitively detect modified peptides and identify the site and nature of a number of protein modifications in parallel. We have demonstrated the utility of this method by characterizing for the first time oxidized phospholipid adducts to LDL and human serum albumin and for the detection of glycosylation and kynurenin formation from the oxidation of tryptophan residues in LDL." @default.
- W2094576754 created "2016-06-24" @default.
- W2094576754 creator A5007439444 @default.
- W2094576754 creator A5035356657 @default.
- W2094576754 creator A5064011950 @default.
- W2094576754 date "2013-04-23" @default.
- W2094576754 modified "2023-09-25" @default.
- W2094576754 title "Use of Narrow Mass-Window, High-Resolution Extracted Product Ion Chromatograms for the Sensitive and Selective Identification of Protein Modifications" @default.
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- W2094576754 doi "https://doi.org/10.1021/ac400131f" @default.
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