Expression and enzymatic activity of recombinant cytochrome P 450 17 a-hydroxylase in Escherichia coli ( steroid hydroxylase / bacterial expression / reductase )

@inproceedings{BarnesExpressionAE,
  title={Expression and enzymatic activity of recombinant cytochrome P 450 17 a-hydroxylase in Escherichia coli ( steroid hydroxylase / bacterial expression / reductase )},
  author={Henry J. Barnes and M P Arlotto and Michael R. Waterman}
}
When the cDNA encoding bovine microsomal 17a-hydroxylase cytochrome P450 (P45017a) containing modifications within the first seven codons which favor expression in Escherichia coli is placed in a highly regulated tac promoter expression plasmid, as much as 16 mg of spectrally detectable P45017a per liter of culture can be synthesized and integrated into E. coli membranes. The known enzymatic activities of bovine P45017a can be reconstituted by addition of purified rat liver NADPH-cytochrome… CONTINUE READING

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