Expression of truncated forms of liver microsomal P450 cytochromes 2B4 and 2E1 in Escherichia coli: influence of NH2-terminal region on localization in cytosol and membranes.

@article{Pernecky1993ExpressionOT,
  title={Expression of truncated forms of liver microsomal P450 cytochromes 2B4 and 2E1 in Escherichia coli: influence of NH2-terminal region on localization in cytosol and membranes.},
  author={Steven J. Pernecky and Jacinda R Larson and Richard M. Philpot and Minor J. Coon},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1993},
  volume={90 7},
  pages={2651-5}
}
The currently accepted model for the membrane topology of microsomal cytochrome P450 is that of a largely cytoplasmic domain bound by only one or two transmembrane segments at the NH2 terminus. However, as we have reported previously, P450 2E1 lacking the hydrophobic NH2-terminal signal peptide, like the full-length protein, is located in the inner cell membrane when expressed in Escherichia coli and is active with typical substrates. In the present study, additional variants of alcohol… CONTINUE READING
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