Control of aggregation in protein refolding: the temperature-leap tactic.

@article{Xie1996ControlOA,
  title={Control of aggregation in protein refolding: the temperature-leap tactic.},
  author={Yongshu Xie and D. B. Wetlaufer},
  journal={Protein science : a publication of the Protein Society},
  year={1996},
  volume={5 3},
  pages={517-23}
}
The kinetics of renaturation of bovine carbonic anhydrase II (CAII) were studied from 4 degrees to 36 degrees, at the relatively high [CAII] of 4 mg/mL. Following dilution to 1 M guanidinium chloride, aggregate formation is very rapid and reduces the formation of active enzyme. The CAII activity yield at 150 min, 20 degrees (approximately 60%), is greater than that at either 4 degrees or 36 degrees. However, if refolding is conducted at 4 degrees, aggregation is reduced dramatically and 37… CONTINUE READING

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