Chemical modification of proteins by methylglyoxal.

@article{Degenhardt1998ChemicalMO,
  title={Chemical modification of proteins by methylglyoxal.},
  author={Thorsten P Degenhardt and Suzanne R. Thorpe and John W. Baynes},
  journal={Cellular and molecular biology},
  year={1998},
  volume={44 7},
  pages={1139-45}
}
Methylglyoxal is formed in vivo by spontaneous decomposition of triose phosphate intermediates in aerobic glycolysis. It may also be formed during oxidative degradation of both carbohydrates (pentoses and ascorbate) and lipids (arachidonate). In addition to reaction with arginine residues to form imidazolone adducts, methylglyoxal reacts with lysine residues in protein to form N(epsilon)-(carboxyethyl)lysine (CEL) and the imidazolium crosslink, methylglyoxal-lysine dimer (MOLD). Like the… CONTINUE READING

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