Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element.

@article{Chong1997SinglecolumnPO,
  title={Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element.},
  author={Shaorong Chong and Fana B Mersha and Donald Comb and Mark E Scott and David Landry and Luis Vence and Francine B. Perler and Jack Benner and Rebecca B Kucera and Christine A Hirvonen and J. J. Pelletier and Henry Paulus and Ming Q. Xu},
  journal={Gene},
  year={1997},
  volume={192 2},
  pages={271-81}
}
A novel protein purification system has been developed which enables purification of free recombinant proteins in a single chromatographic step. The system utilizes a modified protein splicing element (intein) from Saccharomyces cerevisiae (Sce VMA intein) in conjunction with a chitin-binding domain (CBD) from Bacillus circulans as an affinity tag. The concept is based on the observation that the modified Sce VMA intein can be induced to undergo a self-cleavage reaction at its N-terminal… CONTINUE READING

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