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1 Polish Journal of Chemistry

1 1999

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Model Studies of the Maillard Reaction of Arg-Lys with D-Glucose

Al-Abed Y., Callaway D., Kapurniotu A., Holak T., Voelter W.

Polish Journal of Chemistry

1999

vol. 73 nr 1

117-123

Possible routes leading from Amadori product presusors to glucose-derived protein crosslinks has been suggested by model studies examining the fate of the Amadori products in vitro. For instance, the Amadori product can undergo dehydration to give 1,4 dideoxy-1-alkylamino-2,3-hexodiulose (AP-dione), which has been isolated by trapping with aminoguanidine. In a model reaction, we selected as an AGE target the dipeptide Na-Z-arg-lys. The proximity of the arginine and lysine residues to each other promotes stable intramolecular crosslink formation. Incubation of Na-Z-arg-lys with 10 equivalents of glucose in 0.2 M phosphate buffer (pH 7,4) at 37oC for five weeks produces at least 25 distinct reaction products upon fractionaction of this mixture by HPLC. Each fraction was isolated, concentrated, and analyzed for its reactivity with a polyclonal anti-AGEs that increase as a consequence of hyperglycemia and which are inhibited from forming in human subjects by treatment with the advanced glycation inhibitor aminoguanidine. The products present within one fraction (1.5% yield) were found to block antibody binding in a dose-dependent fashion. Further purification of this fraction by HPLC revealed the presence of one major (0.6% yield) immunoreactive compound. Characterization of this adduct by UV, ESMS and 1H-NMR spectra revealed the presence of intramolecular arg-lys-imidazole crosslink. This crosslink is non-fluorescent and acid labile and may represent an important class of immunoreactive AGE-crosslinks that form in vivo.