Unfolding and refolding of bovine serum albumin at acid pH: ultrasound and structural studies.

@article{Kadi2006UnfoldingAR,
  title={Unfolding and refolding of bovine serum albumin at acid pH: ultrasound and structural studies.},
  author={N El Kadi and Nicolas Taulier and J-Y Le Hu{\'e}rou and Marcel Gindre and Wladimir Urbach and I Nwigwe and Peter C. Kahn and Marcel Waks},
  journal={Biophysical journal},
  year={2006},
  volume={91 9},
  pages={
          3397-404
        }
}
Serum albumin is the most abundant protein in the circulatory system. The ability of albumins to undergo a reversible conformational transition, observed with changes in pH, is conserved in distantly related species, suggesting for it a major physiological role possibly related to the transport of small molecules including drugs. We have followed changes of bovine serum albumin (BSA) in volume by densimetry and in adiabatic compressibility during its conformational transition from pH 7-2, using… CONTINUE READING

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