Issue 84, 2013
From the journal:

Chemical Communications

A highly selective probe for human cytochrome P450 3A4: isoform selectivity, kinetic characterization and its applications†

Guang-Bo Ge,‡a   Jing Ning,‡ab   Liang-Hai Hu,‡c   Zi-Ru Dai,a   Jie Hou,b   Yun-Feng Cao,a   Zhen-Wen Yu,a   Chun-Zhi Ai,a   Jing-Kai Gu,c   Xiao-Chi Ma*b  and  Ling Yang*a  

* Corresponding authors

a Laboratory of Pharmaceutical Resource Discovery, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, China
E-mail: ylingdicp@gmail.com

b Dalian Medical University, Dalian, China
E-mail: maxc1978@163.com

c Research Center for Drug Metabolism, College of Life Science, Jilin University, Changchun, China

Abstract

Bufalin 5β-hydroxylation was found to be an isoform-specific biotransformation probe substrate for cytochrome P450 3A4 (CYP3A4). The probe reaction was well-characterized and it can be used for measuring the real catalytic activities of CYP3A4 from different enzyme sources.

Graphical abstract: A highly selective probe for human cytochrome P450 3A4: isoform selectivity, kinetic characterization and its applications

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Article information

DOI
https://doi.org/10.1039/C3CC45250F
Article type
Communication
Submitted
12 Jul 2013
Accepted
16 Aug 2013
First published
20 Aug 2013

Chem. Commun., 2013,49, 9779-9781

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A highly selective probe for human cytochrome P450 3A4: isoform selectivity, kinetic characterization and its applications

G. Ge, J. Ning, L. Hu, Z. Dai, J. Hou, Y. Cao, Z. Yu, C. Ai, J. Gu, X. Ma and L. Yang, Chem. Commun., 2013, 49, 9779 DOI: 10.1039/C3CC45250F

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