Enthalpic destabilization of glycosylated lysozymes constructed by genetic modification.

@article{Kato2000EnthalpicDO,
  title={Enthalpic destabilization of glycosylated lysozymes constructed by genetic modification.},
  author={A. Kato and S. Nakamura and M. Ban and H. Azakami and K. Yutani},
  journal={Biochimica et biophysica acta},
  year={2000},
  volume={1481 1},
  pages={
          88-96
        }
}
  • A. Kato, S. Nakamura, +2 authors K. Yutani
  • Published 2000
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • To understand the role of polyglycosylation in protein stability, the thermodynamic changes in the denaturation of various polymannosyl lysozyme mutants (R21T, G49N, R21T/G49N) constructed by genetic modification were analyzed using differential scanning calorimetry (DSC). The denaturation temperature and the enthalpy change for unfolding of the lysozymes were reduced with an increase in the length of the polymannose chain and the number of binding sites to a protein, although the polymannosyl… CONTINUE READING
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