Engineering a reversible, high-affinity system for efficient protein purification based on the cohesin-dockerin interaction.

@article{Karpol2009EngineeringAR,
  title={Engineering a reversible, high-affinity system for efficient protein purification based on the cohesin-dockerin interaction.},
  author={Alon Karpol and Lia Kantorovich and Alik Demishtein and Yoav Barak and Ely Morag and Raphael Lamed and Edward A Bayer},
  journal={Journal of molecular recognition : JMR},
  year={2009},
  volume={22 2},
  pages={91-8}
}
Efficient degradation of cellulose by the anaerobic thermophilic bacterium, Clostridium thermocellum, is carried out by the multi-enzyme cellulosome complex. The enzymes on the complex are attached in a calcium-dependent manner via their dockerin (Doc) module to a cohesin (Coh) module of the cellulosomal scaffoldin subunit. In this study, we have optimized the Coh-Doc interaction for the purpose of protein affinity purification. A C. thermocellum Coh module was thus fused to a carbohydrate… CONTINUE READING
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