Refolding of bovine threonine-neochymotrypsinogen.

@article{Duda1982RefoldingOB,
  title={Refolding of bovine threonine-neochymotrypsinogen.},
  author={C. Duda and A. Light},
  journal={The Journal of biological chemistry},
  year={1982},
  volume={257 16},
  pages={
          9866-71
        }
}
  • C. Duda, A. Light
  • Published 1982
  • Medicine, Chemistry
  • The Journal of biological chemistry
The mixed disulfide derivative of fully reduced neochymotrypsinogen was refolded at pH 9.2 and 4 degrees C with 4 mM cysteine as the disulfide interchange catalyst. The yield of regenerated neochymotrypsinogen was 25%; the corresponding yield of refolded chymotrypsinogen was 50%. The refolded neochymotrypsinogen exhibited the characteristics of the native molecule as determined from polyacrylamide gel electrophoresis and the enzymatic properties of the activated zymogen. The rate of refolding… Expand
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