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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2002.9
- 수록면
- 249 - 257 (9page)
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Cytochrome P450 3As such as 3A4 and 3A5 metaboize a wide range of pharmaceutical compounds. The vectors for the expression of fusion proteins containing an N-termical human P450 3A4 or P450 3A5 sequences and a C-termical rat NADPH-cytochrome P450 reductase moiety were constructed. These plasmide were used to express the fusion proteins in Escherichia coli DH5α cells. High levels of expression were achieved (100~200 nmol/liter) and the expressed fusion proteins in E. coli membranes were catalytically active for nifedipine oxidation, a typical enzymatic activity of P450 3A4. The NADPH-P450 reductase activities of these fusion proteins were also determined by measuring reduction of cytochrome c. To find a specific inhibitor of P450 3A4 from naturally accurring chemicals, a series of isothiocyanate compounds were evaluated for the inhibitory activity of P450 using the fusion proteins in E. coli membranes. Of the five isothiocyanates (phenethyl isothiocynate, phenyl isothiocyanate, benzyl isothiocyanate, benzoyl isothiocyanate and cyclohexyl isothiocyanate) tested, benzoyl isothiocyanate showed a strong inhibition of P450 3A4 with an IC_(50) value of 2.8μM. Our results indicate that the self-sufficient fusion proteins will be very useful tool to study the drug metabolism and benzyl isothiocyanate may be valuable for characterizing the enzymatic properties of P450 3A4.
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