NADH oxidation during peroxidase catalyzed metabolism of carcinogenic non-aminoazo dye 1-phenylazo-2-hydroxynaphthalene (Sudan I)

1990 ◽  
Vol 55 (9) ◽  
pp. 2321-2327 ◽  
Author(s):  
Marie Stiborová ◽  
Pavel Anzenbacher
Keyword(s):  
Nucleic Acids ◽  
Chemical Carcinogenesis ◽  
Point Of View ◽  
Nadh Oxidation ◽  
Physiological Significance ◽  
Reactive Metabolite ◽  
Sudan I ◽  
Catalyzed Oxidation

The peroxidase catalyzed oxidation of 1-phenylazo-2-hydroxynaphthalene (Sudan I) in the presence of NADH results in oxidation to oxidized NAD+. This oxidation is supposed to be caused by the reduction of reactive Sudan I metabolite(s). Under certain conditions NADH acts as the agent protecting the cellular nucleophilic compounds such as nucleic acids (DNA, tRNA) against modification caused by reactive metabolite(s) formed from carcinogenic Sudan I by the peroxidase/H2O2 system. The results are discussed from the point of view of the physiological significance of NADH in the initiation of chemical carcinogenesis.

Carcinogenic Non-Aminoazo Dye 1-Phenylazo-2-hydroxynaphthalene (Sudan I) Is Oxidized by Rat Liver Microsomal Cytochrome P-450 to Metabolites Binding to Macromolecules (Nucleic Acids and Proteins)

1992 ◽  
Vol 57 (7) ◽  
pp. 1537-1546 ◽  
Author(s):  
Marie Stiborová ◽  
Pavel Anzenbacher
Keyword(s):  
Nucleic Acids ◽  
Rat Liver ◽  
Chemical Carcinogenesis ◽  
Reactive Metabolites ◽  
Reactive Metabolite ◽  
Microsomal Cytochrome ◽  
Sudan I ◽  
Cytochrome P 450

Carcinogenic non-aminoazo dye 1-phenylazo-2-hydroxynaphthalene (Sudan I) is oxidized by microsomal cytochromes P-450 to reactive metabolite(s) binding to macromolecules (nucleic acids, proteins) in vitro. The extent of binding to macromolecules proceeded in the order: protein > rRNA > tRNA > DNA. The patern of products formed from Sudan I and binding of the reactive metabolites of this compound to macromolecules are dependent on the concentration of Sudan I, NADPH and on the duration of the incubation. The participation of the adducts formed with macromolecules in the initiation of chemical carcinogenesis is discussed.

Chemical Carcinogenesis: Interactions of Carcinogens with Nucleic Acids

1975 ◽  
pp. 235-287 ◽  
Author(s):  
D. S. R. Sarma ◽  
S. Rajalakshmi ◽  
Emmanuel Farber
Keyword(s):  
Nucleic Acids ◽  
Chemical Carcinogenesis

Detoxication products of the carcinogenic azodye Sudan I (Solvent Yellow 14) bind to nucleic acids after activation by peroxidase

1993 ◽  
Vol 68 (1) ◽  
pp. 43-47 ◽  
Author(s):  
Marie Stiborová ◽  
Eva Frei ◽  
Heinz H. Schmeiser ◽  
Manfred Wiessler ◽  
Jan Hradec
Keyword(s):  
Nucleic Acids ◽  
Sudan I

Cytochrome P-450 from Tulip Bulbs (Tulipa fosteriana L.) Oxidizes an Azo Dye Sudan I (1-Phenylazo-2-hydroxynaphthalene, Solvent Yellow 14) in vitro

1996 ◽  
Vol 61 (11) ◽  
pp. 1689-1696
Author(s):  
Marie Stiborová ◽  
Hana Hansíková
Keyword(s):  
Azo Dye ◽  
Microsomal Fraction ◽  
Point Of View ◽  
Transport Chain ◽  
Sudan I ◽  
Tulip Bulbs ◽  
Metabolism Of Xenobiotics ◽  
Cytochrome P 450

The microsomal fraction from tulip bulbs (Tulipa fosteriana L.) contains cytochrome P-450 enzymes catalyzing the NADPH-dependent oxidation of the xenobiotic substrate, an azo dye Sudan I (1-phenylazo-2-hydroxynaphthalene, Solvent Yellow 14). C-Hydroxy derivatives [1-(4-hydroxyphenylazo)-2-hydroxynaphthalene, 1-phenylazo-2,6-dihydroxynaphthalene, 1-(4-hydroxyphenylazo)-2,6-dihydroxynaphthalene] and the benzenediazonium ion are the products of the Sudan I oxidation. The oxidation of Sudan I has also been assessed in a reconstituted electron-transport chain with the isolated cytochrome P-450, isolated plant NADPH-cytochrome P-450 reductase and phospholipid. The results are discussed from the point of view of the role of cytochromes P-450 in the metabolism of xenobiotics in plants.

Mechanism of Formation of (Deoxy)guanosine Adducts Derived from Peroxidase-Catalyzed Oxidation of the Carcinogenic Nonaminoazo Dye 1-Phenylazo-2-hydroxynaphthalene (Sudan I)

2009 ◽  
Vol 22 (11) ◽  
pp. 1765-1773 ◽  
Author(s):  
Martin Dračínský ◽  
Josef Cvačka ◽  
Marcela Semanská ◽  
Václav Martínek ◽  
Eva Frei ◽  
...  
Keyword(s):  
Mechanism Of Formation ◽  
Sudan I ◽  
Catalyzed Oxidation

Exploring the conformational heterogeneity of biomolecules: theory and experiments

2016 ◽  
Vol 18 (8) ◽  
pp. 5684-5685 ◽  
Author(s):  
Claudio Luchinat
Keyword(s):  
Nucleic Acids ◽  
Recent Progress ◽  
Point Of View ◽  
Conformational Heterogeneity ◽  
Theoretical Point ◽  
Conformational Variability ◽  
Theory And Experiments

This themed collection reports on recent progress in the investigation of the conformational variability of biomolecules (proteins and nucleic acids), both from an experimental and theoretical point of view.

scholarly journals Existing Biosensing Platforms for the Nucleotide Markers Detection

2016 ◽  
Author(s):  
Elena Dmitrienko ◽  
Inna Pyshnaya ◽  
Fedor Dultsev ◽  
Andrey Tronin ◽  
Dmitrii Pyshnyi
Keyword(s):  
Nucleic Acids ◽  
Point Of View ◽  
Hybridization Analysis ◽  
Piezoelectric Sensors ◽  
Detection Methods ◽  
Probe Target ◽  
Central Focus

In review, the operating principles of the most common bio sensing devices, detection methods and the identification sensitivity of analyzed molecules were shown. The central focus was done on hybridization analysis of nucleic acids (NA), which are considered to be one of the most important analytes in terms of diagnostic point of view. Constructions enabling to transfer the fact of formation of nucleotide probe/target complex in to detectable signal by optical, electrochemical or micromechanical (piezoelectric) sensors were presented in this review.

New insights into the molecular mechanisms of chemical carcinogenesis: In vivo adduction of histone H2B by a reactive metabolite of the chemical carcinogen furan

2016 ◽  
Vol 264 ◽  
pp. 106-113 ◽  
Author(s):  
João Nunes ◽  
Inês L. Martins ◽  
Catarina Charneira ◽  
Igor P. Pogribny ◽  
Aline de Conti ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Chemical Carcinogenesis ◽  
Reactive Metabolite ◽  
Chemical Carcinogen ◽  
Histone H2b
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