The domain organization of streptokinase: nuclear magnetic resonance, circular dichroism, and functional characterization of proteolytic fragments.

@article{Parrado1996TheDO,
  title={The domain organization of streptokinase: nuclear magnetic resonance, circular dichroism, and functional characterization of proteolytic fragments.},
  author={J Parrado and F Conejero-Lara and Roberts A. Smith and Jean M. Marshall and Chris Paul Ponting and Christopher M. Dobson},
  journal={Protein science : a publication of the Protein Society},
  year={1996},
  volume={5 4},
  pages={693-704}
}
Streptococcus equisimilis streptokinase (SK) is a bacterial protein of unknown tertiary structure and domain organization that is used extensively to treat acute myocardial infarction following coronary thrombosis. Six fragments of SK were generated by limited proteolysis with chymotrypsin and purified. NMR and CD experiments have shown that the secondary and tertiary structure present in the native molecule is preserved within all fragments, except the N-terminal fragment SK7. NMR spectra… CONTINUE READING
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