Comparison of in vitro protein modification with advanced glycation endproduct (AGE) precursors methylglyoxal, glyoxal, 3-deoxyglucosone and glucose using mass spectrometry

International Congress Series

Volumn 1245, Issue C, 2002, Pages 353-354

  Millar, D J ^a   Taylor, G W ^b   Thornalley, P J ^c   Holmes, C ^d   Dawnay, A ^a  

^a QUEEN MARY UNIVERSITY OF LONDON   (United Kingdom)

^b HAMMERSMITH HOSPITAL   (United Kingdom)

^c UNIVERSITY OF ESSEX   (United Kingdom)

^d BAXTER HEALTHCARE CORPORATION   (United States)

Author keywords

3 Deoxyglucosone; AGE precursors; Glyoxal; Methylglyoxal; Protein modification

Indexed keywords

EID: 77955450891     PISSN: 05315131     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0531-5131(02)00899-3     Document Type: Article

References (3)

1. Dawnay, A., Millar, D.J., The pathogenesis and consequences of AGE formation in uraemia and its treatment. Cell. Mol. Biol. 44:7 (1998), 1081-1094.
2. Mann, V.M., Tucker, B., Thornalley, P.J., Dawnay, A., Elevated serum methylglyoxal and glyoxal in uraemia: implications for advanced glycation endproduct formation. Kidney Int., 52, 1999, 2582.
3. Westwood, M.E., Thornalley, P.J., Molecular characteristics of methylglyoxal modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation endproduct modified serum albumins. J. Protein Chem. 14 (1995), 359-372.