Monoclonal antibodies against human cytochrome P-450

1986 ◽  
Vol 14 (3) ◽  
pp. 621-621 ◽  
Author(s):  
TRISTAN S. BARNES ◽  
PETER M. SHAW ◽  
M. DANNY BURKE ◽  
WILLIAM T. MELVIN
Keyword(s):  
Monoclonal Antibodies ◽  
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.

The localization of cytochrome P-450 in normal and pathological human liver by monoclonal antibodies to human cytochrome P-450

1987 ◽  
Vol 15 (4) ◽  
pp. 677-678 ◽  
Author(s):  
G. I. MURRAY ◽  
T. S. BARNES ◽  
S. W. B. EWEN ◽  
H. F. SEWELL ◽  
W. T. MELVIN ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Human Liver ◽  
Human Cytochrome ◽  
Cytochrome P 450

scholarly journals Differences in adult and foetal human cytochrome P-450 forms recognized by monoclonal antibodies with specificity for the P450III family

1989 ◽  
Vol 260 (3) ◽  
pp. 635-640 ◽  
Author(s):  
T S Barnes ◽  
M D Burke ◽  
W T Melvin
Keyword(s):  
Monoclonal Antibodies ◽  
Polyacrylamide Gel Electrophoresis ◽  
Liver Microsomes ◽  
Covalent Modification ◽  
Adult Liver ◽  
Human Adult ◽  
Human Cytochrome ◽  
Foetal Liver ◽  
Cytochrome P 450 ◽  
Murine Monoclonal Antibodies

Six murine monoclonal antibodies raised against a major human adult liver cytochrome P-450 (P-450) of the PCN family (P450III) detected a protein in human foetal liver microsomes (microsomal fractions) which had an approx. 1 kDa higher molecular mass on SDS/polyacrylamide-gel electrophoresis than the protein recognized in human adult liver microsomes. Although each of the antibodies recognized both the adult and the foetal forms, antibody HL4 showed higher affinity for the foetal form. Recognition by the monoclonal antibodies of peptides generated by proteolytic cleavage of microsomal proteins showed different patterns for the adult and foetal forms. It is concluded that the foetal P-450 form recognized by antibodies to the major human adult liver form P450hA7, although structurally similar, is either a distinct P-450 isoenzyme or that the adult and foetal proteins have different covalent modification. Immunoquantification experiments showed comparable levels of the P-450 forms in adult and foetal liver, although there appeared to be less inter-individual variation in foetal livers.

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.

Cytochrome P-450 Function Analyses with Monoclonal Antibodies and cDNA Expression Vectors

1988 ◽  
pp. 3-15
Author(s):  
Harry V. Gelboin ◽  
Frank J. Gonzalez ◽  
Sang S. Park ◽  
Junji Sagara ◽  
Narayana Battula
Keyword(s):  
Monoclonal Antibodies ◽  
Expression Vectors ◽  
Cdna Expression ◽  
Cytochrome P 450

Inhibitory monoclonal antibodies to human cytochrome P450 1A2: analysis of phenacetin O-deethylation in human liver

1998 ◽  
Vol 8 (5) ◽  
pp. 375-382 ◽  
Author(s):  
Tian J. Yang ◽  
Yang Sai ◽  
Kristopher W. Krausz ◽  
Frank J. Gonzalez ◽  
Harry V. Gelboin
Keyword(s):  
Cytochrome P450 ◽  
Monoclonal Antibodies ◽  
Human Liver ◽  
Cytochrome P450 1A2 ◽  
Human Cytochrome

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

Cross-reactivity of thirteen monoclonal antibodies with ten vaccinia cDNA expressed rat, mouse and human cytochrome P450s

1993 ◽  
Vol 46 (5) ◽  
pp. 787-790 ◽  
Author(s):  
Inna Goldfarb ◽  
Kenneth Korzekwa ◽  
Kristopher W. Krausz ◽  
Frank Gonzalez ◽  
Harry V. Gelboin
Keyword(s):  
Monoclonal Antibodies ◽  
Cross Reactivity ◽  
Cytochrome P450s ◽  
Human Cytochrome
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