Co-expression of human cytochrome b(5) increases expression of cytochrome P450 3A4 in Escherichia coli by stabilizing mRNA
- Authors
- Dong, Mi-Sook; Lee, Sang-Bum; Kim, Hyun-Jung
- Issue Date
- 5월-2013
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Co-expression of CYP3A4; NADPH-cytochrome P450 reductase; Cytochrome b(5); mRNA stabilization; Stationary phase of E. coli
- Citation
- PROTEIN EXPRESSION AND PURIFICATION, v.89, no.1, pp.44 - 50
- Indexed
- SCIE
SCOPUS
- Journal Title
- PROTEIN EXPRESSION AND PURIFICATION
- Volume
- 89
- Number
- 1
- Start Page
- 44
- End Page
- 50
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/103463
- DOI
- 10.1016/j.pep.2013.02.010
- ISSN
- 1046-5928
- Abstract
- CYP3A4 is the most abundant cytochrome P450 in the human liver. The expression level of CYP3A4 when coexpressed with cytochrome b(5) (cyt b(5)) in Escherichia coli was 20-60% higher than that when it was expressed alone over an extended period (48-72 h). This time-dependent elevation in coexpression with cyt b(5) 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 b(5) primarily resulted from CYP3A4 mRNA stabilization by cyt b(5). (C) 2013 Elsevier Inc. All rights reserved.
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