The oxidative modification of human hemoglobin (Hb) treated with hydrogen peroxide was investigated. Using the mass spectrometry method, the oxidized amino acid residues of the hemoglobin molecule were detected: αTrp14, αTyr24, αArg31, αMet32, αTyr42, αHis45, αHis72, αMet76, αPro77, αLys90, αCys104, αTyr140, βHis2, βTrp15, βTrp37, βMet55, βCys93, βCys112, βTyr130, βLys144, and βHis146. The antioxidant potential of the Hb molecule in the intracellular space and in the blood plasma is discussed.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1134/S1607672919030116 | DOI Listing |
Publication Analysis
Top Keywords
oxidative modification
8
peroxide-induced oxidative
4
modification hemoglobin
4
hemoglobin oxidative
4
modification human
4
human hemoglobin
4
hemoglobin treated
4
treated hydrogen
4
hydrogen peroxide
4
peroxide investigated
4
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!