Transition metals bind to glycated proteins forming redox active "glycochelates": implications for the pathogenesis of certain diabetic complications.

@article{Qian1998TransitionMB,
  title={Transition metals bind to glycated proteins forming redox active "glycochelates": implications for the pathogenesis of certain diabetic complications.},
  author={Mei-rong Qian and Ming-yih Liu and John W. Eaton},
  journal={Biochemical and biophysical research communications},
  year={1998},
  volume={250 2},
  pages={385-9}
}
The present investigations arose from our interest in the possibility that some structures which arise secondary to protein glycation might bind transition metals such as iron and copper. In support of this we find that, when glycated, three different proteins--albumin, gelatin (a soluble collagen fragment) and elastin--all gain a substantial affinity for the transition metals iron and copper. The glycated proteins bind at least three times as much iron as do the non-glycated proteins… CONTINUE READING

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