Human cytochrome P-450 enzymes

Life Sciences ◽  
1992 ◽  
Vol 50 (20) ◽  
pp. 1471-1478 ◽  
Author(s):  
F. Peter Guengerich
Keyword(s):  
Human Cytochrome ◽  
Cytochrome P 450

scholarly journals Thermodynamic studies of substrate binding and spin transitions in human cytochrome P-450 3A4 expressed in yeast microsomes

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
Keyword(s):  
Thermodynamic Parameters ◽  
Protein Interactions ◽  
Substrate Binding ◽  
Principal Component ◽  
Yeast Saccharomyces Cerevisiae ◽  
Human Cytochrome ◽  
Different Temperatures ◽  
Haem Protein ◽  
Cytochrome P 450 ◽  
Spin Transitions

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.

Isolation of a human cytochrome P-450 reductase cDNA clone and localization of the corresponding gene to chromosome 7q11.2

1989 ◽  
Vol 53 (4) ◽  
pp. 291-301 ◽  
Author(s):  
E. A. SHEPHARD ◽  
I. R. PHILLIPS ◽  
I. SANTISTEBAN ◽  
L. F. WEST ◽  
C. N. A. PALMER ◽  
...  
Keyword(s):  
Cdna Clone ◽  
Human Cytochrome ◽  
Cytochrome P 450

Identification of human cytochrome P 450 s that metabolise anti-parasitic drugs and predictions of in vivo drug hepatic clearance from in vitro data

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
Keyword(s):  
Hepatic Clearance ◽  
Human Cytochrome ◽  
Cytochrome P 450 ◽  
Vitro Data ◽  
In Vitro Data

scholarly journals Effects of Furanocoumarins from Apiaceous Vegetables on the Catalytic Activity of Recombinant Human Cytochrome P-450 1A2

2011 ◽  
Vol 30 (7) ◽  
pp. 447-456 ◽  
Author(s):  
Ah-Young Kang ◽  
Lindsay R. Young ◽  
Carlus Dingfelder ◽  
Sabrina Peterson
Keyword(s):  
Catalytic Activity ◽  
Human Cytochrome ◽  
Cytochrome P 450

Gene Structure of Human Cytochrome P-450(SCC), Cholesterol Desmolase

1987 ◽  
Vol 101 (4) ◽  
pp. 879-887 ◽  
Author(s):  
Ken-ichirou MOROHASHI ◽  
Kazuhiro SOGAWA ◽  
Tsuneo OMURA ◽  
Yoshiaki FUJII-KURIYAMA
Keyword(s):  
Gene Structure ◽  
Human Cytochrome ◽  
Cytochrome P 450

scholarly journals Monoclonal antibodies against human cytochrome P-450 recognizing different pregnenolone 16α-carbonitrile-inducible rat cytochromes P-450

1987 ◽  
Vol 248 (1) ◽  
pp. 301-304 ◽  
Author(s):  
T S Barnes ◽  
P M Shaw ◽  
M D Burke ◽  
W T Melvin
Keyword(s):  
Monoclonal Antibodies ◽  
Human Liver ◽  
Liver Microsomes ◽  
Human Liver Microsomes ◽  
The Other ◽  
Male Rat ◽  
Rat Liver Microsomes ◽  
Human Cytochrome ◽  
Male Specific ◽  
Cytochrome P 450

Six murine monoclonal antibodies against human hepatic cytochrome P-450 have been raised, using human liver microsomes (microsomal fractions) or semi-purified human cytochrome P-450 as immunogen. All six antibodies recognized the same highly purified of human liver cytochrome P-450 of molecular mass 53 kDa and gave rise to a single band at 53 kDa on immunoblots of human liver microsomes from 11 individuals. The antibodies also recognized proteins at 52 kDa and 54 kDa on immunoblots of control and induced male-rat liver microsomes, showing four different banding patterns. Antibodies HL4 and HP16 recognized a 52 kDa protein that was only weakly expressed in untreated rats and which was strongly induced by pregnenolone 16 alpha-carbonitrile (PCN) but not by phenobarbitone (PB), 3-methylcholanthrene (3MC), isosafrole (ISF), Aroclor 1254 (ARO), clofibrate or imidazole. HP10 and HL5 recognized a constitutive 52 kDa protein that was weakly induced by PCN but not by the other agents and was suppressed by 3MC and ARO. HP3 recognized a 54 kDa protein that was undetectable in control rats but was strongly induced by PB, PCN, ISF and ARO. HL3 appeared to recognize a combination of the proteins recognized by the other antibodies plus a 54 kDa protein that was weakly expressed in control rats. The constitutive proteins recognized were male-specific.

A human cytochrome P-450 is recognized by anti-liver/kidney microsome antibodies in autoimmune chronic hepatitis

1989 ◽  
Vol 159 (1) ◽  
pp. 283-289 ◽  
Author(s):  
Liliane Kiffel ◽  
Jacqueline Loeper ◽  
Jean Claude Homberg ◽  
Jean Paul Leroux
Keyword(s):  
Chronic Hepatitis ◽  
Human Cytochrome ◽  
Cytochrome P 450 ◽  
Kidney Microsome
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