Controlled oxidative protein refolding using an ion-exchange column.

@article{Langenhof2005ControlledOP,
  title={Controlled oxidative protein refolding using an ion-exchange column.},
  author={Marc Langenhof and Susanna S J Leong and Leonard Keith Pattenden and Anton P. J. Middelberg},
  journal={Journal of chromatography. A},
  year={2005},
  volume={1069 2},
  pages={195-201}
}
Column-based refolding of complex and highly disulfide-bonded proteins simplifies protein renaturation at both preparative and process scale by integrating and automating a number of operations commonly used in dilution refolding. Bovine serum albumin (BSA) was used as a model protein for refolding and oxido-shuffling on an ion-exchange column to give a refolding yield of 55% after 40 h incubation. Successful on-column refolding was conducted at protein concentrations of up to 10 mg/ml and… CONTINUE READING

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This technique integrates the dithiothreitol removal , refolding , concentration and purification steps , achieving a high level of process simplification and automation , and a significant saving in reagent costs when scaled .
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