Characterization of human cytochrome P450 enzymes involved in thein vitro metabolism of perospirone

2005 ◽  
Vol 26 (2) ◽  
pp. 59-65 ◽  
Author(s):  
Atsushi Kitamura ◽  
Yoshiko Mizuno ◽  
Kiyoshi Natsui ◽  
Masashi Yabuki ◽  
Setsuko Komuro ◽  
...  
2007 ◽  
Vol 35 (9) ◽  
pp. 1634-1641 ◽  
Author(s):  
Khaled Abass ◽  
Petri Reponen ◽  
Miia Turpeinen ◽  
Jorma Jalonen ◽  
Olavi Pelkonen

2007 ◽  
Vol 32 (4-5) ◽  
pp. 357-366 ◽  
Author(s):  
Christophe Arbus ◽  
Amine Benyamina ◽  
Pierre-Michel Llorca ◽  
Franck Baylé ◽  
Norbert Bromet ◽  
...  

Author(s):  
Bhaskar Vemu ◽  
Restituo Tocmo ◽  
Mirielle C. Nauman ◽  
Stephanie A. Flowers ◽  
Jacob P. Veenstra ◽  
...  

2005 ◽  
Vol 10 (1) ◽  
pp. 56-66 ◽  
Author(s):  
Olga V. Trubetskoy ◽  
Jasmin R. Gibson ◽  
Bryan D. Marks

Highly miniaturized P450 screening assays designed to enable facile analysis of P450 drug interactions in a 1536-well plate format with the principal human cytochrome P450 enzymes (CYP3A4, 2D6, 2C9, 2C19, and 1A2) and Vivid® fluorogenic substrates were developed. The detailed characterization of the assays included stability, homogeneity, and reproducibility of the recombinant P450 enzymes and the kinetic parameters of their reactions with Vivid® fluorogenic substrates, with a focus on the specific characteristics of each component that enable screening in a low-volume 1536-well plate assay format. The screening assays were applied for the assessment of individual cytochrome P450 inhibition profiles with a panel of selected assay modifiers, including isozyme-specific substrates and inhibitors. IC50 values obtained for the modifiers in 96- and 1536-well plate formats were similar and comparable with values obtained in assays with conventional substrates. An overall examination of the 1536-well assay statistics, such as signal-to-background ratio and Z′ factor, demonstrated that these assays are a robust, successful, and reliable tool to screen for cytochrome P450 metabolism and inhibition in an ultra-high-throughput screening format. ( Journal of Biomolecular Screening 2005:56-66)


2003 ◽  
Vol 31 (3) ◽  
pp. 497-501 ◽  
Author(s):  
A. Gutierrez ◽  
A. Grunau ◽  
M. Paine ◽  
A.W. Munro ◽  
C.R. Wolf ◽  
...  

Cytochrome P450 reductase (CPR) is a diflavin enzyme responsible for electron donation to mammalian cytochrome P450 enzymes in the endoplasmic reticulum. Dissection of the enzyme into functional domains and studies by site-directed mutagenesis have enabled detailed characterization of the mechanism of electron transfer using stopped-flow and equilibrium-perturbation methods, and redox potentiometry. These studies and the mechanism of electron transfer in CPR are reported herein.


Xenobiotica ◽  
2009 ◽  
Vol 39 (1) ◽  
pp. 1-10 ◽  
Author(s):  
H. H. Yoo ◽  
N. S. Kim ◽  
J. Lee ◽  
D. R. Sohn ◽  
C. Jin ◽  
...  

2007 ◽  
Vol 35 (10) ◽  
pp. 1730-1732 ◽  
Author(s):  
Masahiro Hiratsuka ◽  
Yudai Hinai ◽  
Takamitsu Sasaki ◽  
Yumiko Konno ◽  
Kenichi Imagawa ◽  
...  

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