Reversible denaturation of human serum albumin by pH, temperature, and guanidine hydrochloride followed by optical rotation.

@article{Wallevik1973ReversibleDO,
  title={Reversible denaturation of human serum albumin by pH, temperature, and guanidine hydrochloride followed by optical rotation.},
  author={K. Wallevik},
  journal={The Journal of biological chemistry},
  year={1973},
  volume={248 8},
  pages={2650-5}
}
  • K. Wallevik
  • Published 1973 in The Journal of biological chemistry
The pH-dependent transitions and the thermal unfolding of defatted human serum albumin in 0.2 M KC1 as followed by polarimetry at 233 nm are found to be independent processes. The apparent net loss of structure (01 helix) in the unfolding between pH ‘7 and 9 is 2.5%, in the N-F transformation it is 8% and in the acid expansion 1%. The two last mentioned transitions seem to be independent of each other. There is a temperature of maximum stability of the N stage in the N-F transformation at 18… CONTINUE READING
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hoc . Xal . AcacZ

  • N. S. SIMMONS, C. COHEN
  • 1964

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