scholarly journals Identification of Human Cytochrome P-450 involved in a Drug Metabolism and its Application

1994 ◽  
Vol 9 (supplement) ◽  
pp. 210-211
Author(s):  
Noriaki Shimada
PLoS ONE ◽  
2016 ◽  
Vol 11 (7) ◽  
pp. e0160172 ◽  
Author(s):  
Ana Carolina Rios Silvino ◽  
Gabriel Luiz Costa ◽  
Flávia Carolina Faustino de Araújo ◽  
David Benjamin Ascher ◽  
Douglas Eduardo Valente Pires ◽  
...  

PLoS ONE ◽  
2018 ◽  
Vol 13 (2) ◽  
pp. e0192534
Author(s):  
Ana Carolina Rios Silvino ◽  
Gabriel Luiz Costa ◽  
Flávia Carolina Faustino de Araújo ◽  
David Benjamin Ascher ◽  
Douglas Eduardo Valente Pires ◽  
...  

1996 ◽  
Vol 319 (3) ◽  
pp. 675-681 ◽  
Author(s):  
Jean-Paul RENAUD ◽  
Dmitri R. DAVYDOV ◽  
Karel P. M. HEIRWEGH ◽  
Daniel MANSUY ◽  
Gaston HUI BON HOA

An approach to the quantitative spectral analysis of substrate binding and inactivation of cytochrome P-450 in microsomes is described. The method is based on the application of the principal component analysis technique on the Soret-region spectra measured at different temperatures at various concentrations of substrate. This approach allowed us to study the thermodynamic parameters of substrate binding and spin transitions in human cytochrome P-450 3A4 expressed in yeast (Saccharomyces cerevisiae) microsomes. These parameters are discussed in comparison with the values reported earlier by Ristau et al. [(1979) Acta Biol. Med. Ger. 38, 177–185] for rabbit liver cytochrome P-450 2B4 in solution with benzphetamine as a substrate. Our analysis shows the substrate-free states of 2B4 and 3A4 to be very similar. However, substrate binding seems to perturb haem-protein interactions in 3A4 in contrast with 2B4, where the effect of substrate binding on the thermodynamic parameters of spin transitions was insignificant. The implication of the results for the mechanism of substrate-induced spin shift is discussed.


Life Sciences ◽  
1992 ◽  
Vol 50 (20) ◽  
pp. 1471-1478 ◽  
Author(s):  
F. Peter Guengerich

1973 ◽  
Vol 51 (1) ◽  
pp. 6-11 ◽  
Author(s):  
G. C. Becking

The effect of vitamin A status on hepatic drug metabolism was studied in rats. Animals were fed diets with and without vitamin A for 20 and 25 days. Weight gains of control and deficient animals were not significantly different, whereas liver vitamin A levels had decreased to less than 10% of control animals after 20 days and were essentially zero after eating the deficient diet for 25 days. Aniline metabolism in vitro and aminopyrine metabolism in vitro and in vivo were significantly lower in male weanling rats fed a vitamin A deficient diet for 20 days. No alteration in in vitro p-nitrobenzoic acid metabolism was noted after 25 days on the test. Vitamin A deficiency did not alter microsomal protein levels or cytochrome c reductase activity but deficient animals did have a lower microsomal cytochrome P-450 content. Hepatic enzyme activities and cytochrome P-450 levels were restored to values approaching those found in control animals by feeding vitamin A deficient rats the vitamin A containing diet for 21 days. Liver vitamin A levels were markedly increased after re-feeding studies but were still significantly lower than control animals.


1989 ◽  
Vol 53 (4) ◽  
pp. 291-301 ◽  
Author(s):  
E. A. SHEPHARD ◽  
I. R. PHILLIPS ◽  
I. SANTISTEBAN ◽  
L. F. WEST ◽  
C. N. A. PALMER ◽  
...  

2003 ◽  
Vol 59 (5-6) ◽  
pp. 429-442 ◽  
Author(s):  
Xue-Qing Li ◽  
Anders Bj�rkman ◽  
Tommy B. Andersson ◽  
Lars L. Gustafsson ◽  
Collen M. Masimirembwa

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