Counteracting effects of renal solutes on amyloid fibril formation by immunoglobulin light chains.

@article{Kim2001CounteractingEO,
  title={Counteracting effects of renal solutes on amyloid fibril formation by immunoglobulin light chains.},
  author={Young Seog Kim and Stephen P. Cape and Ellen Chi and Rosemarie Raffen and P Wilkins-Stevens and Fred J. Stevens and Mark Cornell Manning and Theodore W. Randolph and Ariel Solomon and John F. Carpenter},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 2},
  pages={
          1626-33
        }
}
In primary (light chain-associated) amyloidosis, immunoglobulin light chains deposit as amyloid fibrils in vital organs, especially the kidney. Because the kidney contains high concentrations of urea that can destabilize light chains as well as solutes such as betaine and sorbitol that serve as protein stabilizers, we investigated the effects of these solutes on in vitro amyloid fibril formation and thermodynamic stability of light chains. Two recombinant light chain proteins, one amyloidogenic… CONTINUE READING

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