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Updated: Jun 17, 2026

Covalent Labeling with Diethylpyrocarbonate for Studying Protein Higher-Order Structure by Mass Spectrometry
Published on: June 15, 2021
Mass spectrometric evidence for the existence of distinct modifications of different proteins by 2(E),4(E)-decadienal
Xiaochun Zhu1, Xiaoxia Tang, Jianye Zhang
1Department of Chemistry and Biochemistry, Case Western Reserve University, Cleveland, Ohio 44106, USA. xiaochun@amgen.com
Abstract:
2(E),4(E)-Decadienal (DDE), a lipid peroxidation product, was found to covalently modify Lys residues of different proteins by different reactions using mass spectrometry (MALDI-TOF-MS and LC-ESI-MS). DDE mainly formed Lys Schiff base adducts with cytochrome c and ribonuclease A at 10 min, but these reversibly formed adducts almost disappeared after 24 h. In contrast, beta-lactoglobulin (beta-LG) was highly modified by DDE after 24 h. In addition to the Lys Schiff base adducts, DDE formed novel Lys pyridinium adducts as well as Cys Michael adducts with beta-LG.
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