Protease digestion studies of an equilibrium intermediate in the unfolding of creatine kinase.

@article{Webb1997ProteaseDS,
  title={Protease digestion studies of an equilibrium intermediate in the unfolding of creatine kinase.},
  author={T I Webb and Pilgrim J Jackson and Glenn E. Morris},
  journal={The Biochemical journal},
  year={1997},
  volume={321 ( Pt 1)},
  pages={83-8}
}
Protease digestion experiments have been used to characterize the structure of an equilibrium intermediate in the unfolding of creatine kinase (CK) by low concentrations (0.625 M) of guanidine hydrochloride (GdnHCl). Eighteen of the major products of digestion by trypsin, chymotrypsin and endoproteinase Glu-C have been identified by microsequencing after separation by SDS/PAGE and electroblotting on poly(vinylidene difluoride) membranes. The C-terminal portion (Gly215 to Lys380) was much more… CONTINUE READING

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