Efficient and Rapid Affinity Purification of Proteins Using Recombinant Fusion Proteases

@article{Walker1994EfficientAR,
  title={Efficient and Rapid Affinity Purification of Proteins Using Recombinant Fusion Proteases},
  author={Philip A. Walker and Louis E. -C. Leong and Patrick Wei Pern Ng and Shyh Han Tan and Sarah Waller and David K. Murphy and A. G. Porter},
  journal={Bio/Technology},
  year={1994},
  volume={12},
  pages={601-605}
}
In the affinity purification of recombinant fusion proteins, the rate-limiting step is usually the efficient proteolytic cleavage and removal of the affinity tail and the protease from the purified recombinant protein. We have developed a rapid, convenient and efficient method of affinity purification which can overcome this limitation. In one example of the method, the protease 3C from a picornavirus (3Cpro), which cleaves specific sequences containing a minimum of 6–7 amino acids, has been… CONTINUE READING

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