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Feasibility of electromigration and gas chromatographic techniques for assessing glycoxidation of proteins

AutorAmigo-Benavent, Miryam; Montilla, Antonia ; Castillo, M. Dolores del
Fecha de publicación2010
CitaciónISC 2010
ResumenAdvanced glycation end products (AGEs) or glycoxidation products are formed via Maillard reaction between reducing sugars and free amino groups of proteins, lipids and nucleic acids. These compounds are formed in foods and in vivo under physiologic conditions and are responsible for diabetes mellitus (DM) and aging complications. One of the most representative AGEs is εN-carboxymethyl-lysine (CML). DM is one of the most important diseases in Western countries. Different compounds such as chlorogenic acid (CGA) from beverages (mate, coffe), several fruits and vegetables may possess antiglycating effect. However, the mechanism of action of CGA against formation of Maillard reaction products in vitro and in vivo has not been established yet. The aim of this research was to develop a method to follow the glycoxidation of biological proteins and to evaluate the protective effect if so of chlorogenic acid against the formation of glycotoxins (carboxymethylated-protein or CML-protein). Glycoxidation model systems based on both human serum albumin (HSA) or human hemoglobulin (Hb) were performed as follow: mL of a protein solution (25 mg/mL of 0.2 M phosphate buffer pH 8) were treated with 360 μL of 0.3 M glyoxylic acid and 360 μL of 0.9 M sodium cyanoborohydride without (glycoxidation sample) and with addition of 100 μL of 0.4 mM CGA (antiglycoxidation sample) at 37ºC with constant stirring at 750 rpm up to 96 hours. Other controls based on protein and CGA alone were also undertaken. Glycoxidation was followed by SDS-PAGE, CZE5 and GC analysis. Data on SDS-PAGE, GC and CZE were compared. Results indicated the feasibility of the three analytical tools to look at protein glycoxidation.
DescripciónResumen del póster presentado al 28th International Symposium on Chromatography celebrado en Valencia (España) del 12 al 16 de septiembre de 2010.
Aparece en las colecciones: (CIAL) Comunicaciones congresos
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