Thermolabile antifreeze protein produced in Escherichia coli for structural analysis.

@article{Lin2012ThermolabileAP,
  title={Thermolabile antifreeze protein produced in Escherichia coli for structural analysis.},
  author={Feng-Hsu Lin and Tianjun Sun and Garth L. Fletcher and Peter L Davies},
  journal={Protein expression and purification},
  year={2012},
  volume={82 1},
  pages={75-82}
}
The only hyperactive antifreeze protein (AFP) found to date in fishes is an extreme variant of the 3-kDa, alpha-helical, alanine-rich type I AFP, which is referred to here as type Ih. Purification of the 33-kDa homodimeric AFP Ih from a natural source was hampered by its low levels in fish plasma; by the need to remove the more abundant smaller isoforms; and by its extreme thermolability. Moreover, ice affinity as a purification tool was spoiled by the tendency of fish IgM antibodies to bind to… CONTINUE READING
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