Expression of rat heme oxygenase in Escherichia coli as a catalytically active, full-length form that binds to bacterial membranes.

@article{Ishikawa1991ExpressionOR,
  title={Expression of rat heme oxygenase in Escherichia coli as a catalytically active, full-length form that binds to bacterial membranes.},
  author={Keiko Ishikawa and Michihiko Sato and Takeshi Yoshida},
  journal={European journal of biochemistry},
  year={1991},
  volume={202 1},
  pages={161-5}
}
A plasmid, pKK-RHO, was constructed by incorporating the coding sequence of a cDNA for rat heme oxygenase into the expression vector pKK233-2. Escherichia coli strain XL1-blue transformed with pKK-RHO produced a catalytically active, full-length heme oxygenase. The 32-kDa native enzyme expressed, was localized in the bacterial membranes, possibly due to the spontaneous membrane-binding properties of a hydrophobic segment in its C-terminal region. During cultivation, a few degraded forms of heme… CONTINUE READING

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