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- W2052508722 abstract "We prepared a soluble monomeric form of bovine cytochrome P450 lanosterol 14alpha-demethylase (CYP51), which in mammals is a ubiquitously expressed membrane protein of the endoplasmic reticulum. We constructed two variants of bovine CYP51 (bCYP51) with different truncations and modifications in their N-terminal membrane-spanning domains. Both of these were expressed in Escherichia coli at levels of 500nmol/l. The protein variants were purified and tested for the solubility in the absence of detergent. Variant bCYP51-d1 exhibited approximately 10-fold better solubility over variant bCYT51-d2. The bCYP51-d1 eluted as a single peak in size-exclusion chromatography, corresponding to its monomeric form. The activity of bCYP51-d1 is similar to that of recombinant human CYP51 with a non-truncated membrane-spanning region. High solubility and low tendency to non-specific oligomer formation make bCYP51-d1 a promising candidate for successful crystallization, which may finally allow the structural determination of this important mammalian enzyme." @default.
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- W2052508722 date "2008-07-01" @default.
- W2052508722 modified "2023-10-15" @default.
- W2052508722 title "Expression of microsomal lanosterol 14α-demethylase (CYP51) in an engineered soluble monomeric form" @default.
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- W2052508722 doi "https://doi.org/10.1016/j.bbrc.2008.04.157" @default.
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