Mass spectrometric characterizations of protein carbonylation: Comparison between three different conditions, oxidation by Cu-II/ascorbic acid, adduction of methyl glyoxal, and adduction of 4-hydroxy-2(E)-nonenal

作者：Maeda Kazuki; Funatsu Hiroyuki; Miyazawa Yuki; Misawa Yasushi; Goto Takaaki; Lee Seon Hwa; Oe Tomoyuki^*

来源：International Journal of Mass Spectrometry, 2014, 373: 72-80.

DOI：10.1016/j.ijms.2014.09.012

• Carbonylation
• Protein
• Oxidative stress
• Reactive oxygen species
• Methylglyoxal
• 4-Hydroxy-2(E)-nonenal

Oxidative stress can cause various protein modifications, mainly carbonylation. There are three major chemical ways to introduce hydrazine reactive carbonyls: (i) direct oxidation by reactive oxygen species (ROS), (ii) adduction of sugars or sugar-related aldehydes, and (iii) adduction of lipid-related aldehydes. Here, we performed a comparative study of three representative conditions: Cu-II/ascorbic acid (AA) (ROS), methylglyoxal (sugar-related), and 4-hydroxy-2(E)-nonenal (HNE) (lipid-related). Insulin beta chain and Girard's reagent P were used as the model protein and hydrazine reagent, respectively. LC/MS analyses of reactions with HNE or Cu-II/AA-treated linoleic acid revealed that protein carbonylation under oxidative stress is the most efficient in the presence of polyunsaturated fatty acids.

• 出版日期2014-11-15