A systematic approach to evaluate the modification of lens proteins by glycation-induced crosslinking.

@article{Lee1999ASA,
  title={A systematic approach to evaluate the modification of lens proteins by glycation-induced crosslinking.},
  author={K W Lee and G Simpson and Beryl J. Ortwerth},
  journal={Biochimica et biophysica acta},
  year={1999},
  volume={1453 1},
  pages={
          141-51
        }
}

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Several amine-containing compounds were tested as inhibitors of crosslinking; however, 2-aminoguanidine was the most effective and the rate of synthesis of Lys-Lys, Lys-Arg, and Lys-His crosslinks was determined by measuring the incorporation of [14C]lysine into specific amino acid homopolymers.
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