Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin.

@article{Delpierrre2004IdentificationOF,
  title={Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin.},
  author={Ghislain Delpierrre and Didier Vertommen and David Communi and Mark H. Rider and Emile van Schaftingen},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 26},
  pages={27613-20}
}
Fructosamine-3-kinase (FN3K) phosphorylates fructosamine residues, leading to their destabilization and their shedding from protein. Support for the occurrence of this deglycation mechanism in intact cells has been obtained by showing that hemoglobin is significantly more glycated when human erythrocytes are incubated with an elevated glucose concentration in the presence of 1-deoxy-1-morpholinofructose (DMF), a cell-permeable inhibitor of FN3K, than in its absence. The aim of this work was to… CONTINUE READING

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