Methylglyoxal-derived hydroimidazolone advanced glycation end-products of human lens proteins.

@article{Ahmed2003MethylglyoxalderivedHA,
  title={Methylglyoxal-derived hydroimidazolone advanced glycation end-products of human lens proteins.},
  author={Naila Ahmed and Paul J. Thornalley and Jens Dawczynski and Sybille Franke and Juergen Strobel and Guenter Stein and George M Haik},
  journal={Investigative ophthalmology & visual science},
  year={2003},
  volume={44 12},
  pages={5287-92}
}
PURPOSE To determine the concentrations of methylglyoxal-derived advanced glycation end-products (AGEs), the hydroimidazolones MG-H1 and -H2, in soluble human lens proteins and compare them with the concentrations of other methylglyoxal-derived AGEs and pentosidine. METHODS Lens protein samples were hydrolyzed enzymatically. AGEs were assayed without derivatization by HPLC with tandem mass spectrometry; the fluorescent AGEs argpyrimidine and pentosidine were assayed by fluorometric detection… CONTINUE READING