Abstract
CYP3A4 is the most abundant cytochrome P450 in the human liver. The expression level of CYP3A4 when coexpressed with cytochrome b5 (cyt b5) in Escherichia coli was 20–60% higher than that when it was expressed alone over an extended period (48–72h). This time-dependent elevation in coexpression with cyt b5 was a result of an increase in CYP3A4 mRNA half-life; no significant change in CYP3A4 degradation was seen in the bacterial protease fraction. These results suggest that the higher CYP3A4 levels observed upon coexpression with cyt b5 primarily resulted from CYP3A4 mRNA stabilization by cyt b5.
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