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- W2148849061 abstract "Catalytically active cytochrome P450 enzymes have been successfully expressed in bacterial, yeast, and mammalian cells. A variety of expression vectors have been used, resulting in both transient and stable expression. The system of choice depends on the goals of a particular project. Factors such as expense, ease of use, and yields required should govern the decision whether to use bacterial, yeast, insect, or mammalian cDNA expression. High-level expression of mammalian P450s in bacteria usually requires modifications of the amino-terminal region of the enzyme. The Escherichia coli P450-OR fusion proteins may also come of age for use in fermentation-production processes for the chemical industry. Many cytochromes P450 have been expressed in yeast, with variable levels of expression. Baculovirus, albeit somewhat tedious in having to individualize expression conditions, can produce high levels of enzyme. The standard mammalian cell expression systems, both transient and stable, have been of tremendous value to drug metabolism and carcinogenesis research and will continue to play a role in these areas." @default.
- W2148849061 created "2016-06-24" @default.
- W2148849061 creator A5073932699 @default.
- W2148849061 creator A5088758708 @default.
- W2148849061 date "1995-04-01" @default.
- W2148849061 modified "2023-10-14" @default.
- W2148849061 title "Cytochromes P450 Expression Systems" @default.
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- W2148849061 doi "https://doi.org/10.1146/annurev.pa.35.040195.002101" @default.
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