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Updated: Jul 5, 2026

Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
Published on: December 12, 2013
The peptide-catalyzed Maillard reaction: characterization of 13C reductones
Leif Alexander Garbe1, Alexander Würtz, Christian T Piechotta
1Technische Universität Berlin, Molecular Analysis, Berlin, Germany. leif-a.garbe@tu-berlin.de
Abstract:
The reaction pathways of amino acids and reducing sugars are now fully understood. The focus in the last few years, however, has turned to the reaction of peptides and proteins with reducing sugars. We have investigated the reaction of gamma-aminobutanoic acid, the heptapeptide Nalpha-Acetyl-Lys-Lys-beta-Ala-Lys-beta-Ala-Lys-Gly, and the model protein beta-casein in Maillard reactions with 1-13C arabinose. Characterization of 13C-labeled acetic acid and norfuraneol by gas chromatography-mass spectrometry and nuclear magnetic resonance revealed new formation pathways. The results demonstrate significant differences in the labeling pattern of the products depending on the amine used, indicating different formation pathways of acetic acid and norfuraneol.
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