• Chemistry, Medicine
  • Published in Blood cells 1988

Does the chemical instability of aspartyl and asparaginyl residues in proteins contribute to erythrocyte aging? The role of protein carboxyl methylation reactions.

@article{Lowenson1988DoesTC,
  title={Does the chemical instability of aspartyl and asparaginyl residues in proteins contribute to erythrocyte aging? The role of protein carboxyl methylation reactions.},
  author={Jonathan D. Lowenson and Steven G. Clarke},
  journal={Blood cells},
  year={1988},
  volume={14 1},
  pages={
          103-18
        }
}
As erythrocytes age in the circulation, their proteins are subjected to a wide variety of spontaneous reactions that lead to the formation of covalent derivatives. In this article, we concentrate on nonenzymatic reactions at aspartyl and asparaginyl residues, both of which are especially vulnerable targets on the protein. These residues can be altered by a combination of deamidation, isomerization, and racemization reactions that form D- and L-aspartyl and D- and L-isoaspartyl residues. We… CONTINUE READING

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