P450 monooxygenase in biotechnology. I. Single-step, large-scale purification method for cytochrome P450 BM-3 by anion-exchange chromatography.

@article{Schwaneberg1999P450MI,
  title={P450 monooxygenase in biotechnology. I. Single-step, large-scale purification method for cytochrome P450 BM-3 by anion-exchange chromatography.},
  author={Ulrich Schwaneberg and A Sprauer and Claudia Schmidt-Dannert and Rolf D. Schmid},
  journal={Journal of chromatography. A},
  year={1999},
  volume={848 1-2},
  pages={149-59}
}
An efficient single-step purification protocol for recombinant cytochrome P450 BM-3 from Bacillus megaterium, expressed in E. coli, was developed. Functional crude protein was obtained by disintegrating induced E. coli DH5 alpha and removing cell debris by centrifugation. After investigating different anion-exchange matrices, elution salts and the elution procedures involving an AKTAexplorer system, adsorption of the crude extract from lysed E. coli to Toyopearl DEAE 650M anion exchanger… CONTINUE READING

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