The role of glycosylation and domain interactions in the thermal stability of human angiotensin-converting enzyme.

@article{ONeill2008TheRO,
  title={The role of glycosylation and domain interactions in the thermal stability of human angiotensin-converting enzyme.},
  author={Hester G. O'Neill and Pierre Redelinghuys and Sylva L. U. Schwager and Edward D. Sturrock},
  journal={Biological chemistry},
  year={2008},
  volume={389 9},
  pages={
          1153-61
        }
}
The N and C domains of somatic angiotensin-converting enzyme (sACE) differ in terms of their substrate specificity, inhibitor profiling, chloride dependency and thermal stability. The C domain is thermally less stable than sACE or the N domain. Since both domains are heavily glycosylated, the effect of glycosylation on their thermal stability was investigated by assessing their catalytic and physicochemical properties. Testis ACE (tACE) expressed in mammalian cells, mammalian cells in the… CONTINUE READING
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