Response to “Malondialdehyde-Induced Post-Translational Modification of Human Hemoglobin”

Although malondialdehyde and methylglyoxal have the same molecular formula, they have different chemistry in forming protein adducts. The major lysine adduct of malondialdehyde in hemoglobin is the N-propenal type, while that of methylglyoxal is N 6-(1-carboxyethyl)­lysine. This Letter provides evid...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Journal of proteome research 2023-06, Vol.22 (6), p.2144-2148
Hauptverfasser: Chen, Hauh-Jyun Candy, Liao, Yan-Ling
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:Although malondialdehyde and methylglyoxal have the same molecular formula, they have different chemistry in forming protein adducts. The major lysine adduct of malondialdehyde in hemoglobin is the N-propenal type, while that of methylglyoxal is N 6-(1-carboxyethyl)­lysine. This Letter provides evidence that the “methylglyoxal-like” hemoglobin adducts are not derived from malondialdehyde. This Letter also discusses the quantification of malondialdehyde-induced post-translational modifications in human hemoglobin by different mass spectrometry-based methods.
ISSN:1535-3893
1535-3907
DOI:10.1021/acs.jproteome.3c00073