Peptide Mapping Identifies Hotspot Site of Modification in Human Serum Albumin by Methylglyoxal Involved in Ligand Binding and Esterase Activity

Methylglyoxal is a potent glycating agent under physiological conditions. Human serum albumin is modified by methylglyoxal in vivo. The glycation adducts formed and structural and functional changes induced by methylglyoxal modification have not been fully disclosed. Methylglyoxal reacted with human...

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Veröffentlicht in:	The Journal of biological chemistry 2005-02, Vol.280 (7), p.5724-5732
Hauptverfasser:	Ahmed, Naila, Dobler, Darin, Dean, Mark, Thornalley, Paul J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Binding Sites Cattle Chromatography, Liquid Esterases - chemistry Esterases - metabolism Humans Hydrogen-Ion Concentration Ketoprofen - pharmacology Ligands Mass Spectrometry Models, Molecular Molecular Sequence Data Peptide Mapping Protein Conformation Pyruvaldehyde - chemistry Pyruvaldehyde - pharmacology Serum Albumin - chemistry Serum Albumin - metabolism Trypsin - metabolism
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