Refolding of serine proteinases

@article{Light1986RefoldingOS,
  title={Refolding of serine proteinases},
  author={A. Light and C. Duda and T. W. Odorzynski and W. G. Moore},
  journal={Journal of Cellular Biochemistry},
  year={1986},
  volume={31}
}
Bovine trypsinogen and chymotrypsinogen were successfully refolded as the mixed disulfide of glutathione using cysteine as the disulfide interchange catalyst. The native structures were regenerated with yields of 40%–50% at pH 8.6 and 4 °C, and the half‐time for the refolding was approximately 60–75 min. We then refolded threonine‐neochymotrypsinogen, which is a two‐chain structure held together by disulfide bonds and produced on cleavage of Tyr 146‐Thr 147 in native chymotrypsinogen [Duda CT… Expand
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The mixed disulfide of bovine trypsinogen and glutathione refolded with high yields at protein concentrations of 20 microgram/ml or less, at 4-25 degrees C, pH 8.0 to 8.7, behaved as native trypsInogen as judged by gel exclusion chromatography, isoelectric focusing, and activation with bovines enterokinase or tryps inactivation. Expand
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