Activation of carcinogens by peroxidase. Horseradish peroxidase-mediated formation of benzenediazonium ion from a non-aminoazo dye, 1-phenylazo-2-hydroxynaphthalene (Sudan I) and its binding to DNA
Language English Country Great Britain, England Media print
Document type Journal Article
PubMed
3378630
DOI
10.1016/0014-5793(88)80776-2
PII: 0014-5793(88)80776-2
Knihovny.cz E-resources
- MeSH
- Diazonium Compounds metabolism MeSH
- DNA metabolism MeSH
- Edaravone MeSH
- Antipyrine analogs & derivatives pharmacology MeSH
- Carcinogens MeSH
- Horseradish Peroxidase metabolism MeSH
- Naphthols metabolism MeSH
- Oxidation-Reduction MeSH
- Hydrogen Peroxide MeSH
- Peroxidases metabolism MeSH
- Cattle MeSH
- Spectrophotometry MeSH
- Animals MeSH
- Check Tag
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- 1-phenylazo-2-naphthol MeSH Browser
- benzenediazonium MeSH Browser
- Diazonium Compounds MeSH
- DNA MeSH
- Edaravone MeSH
- Antipyrine MeSH
- Carcinogens MeSH
- Horseradish Peroxidase MeSH
- Naphthols MeSH
- Hydrogen Peroxide MeSH
- Peroxidases MeSH
Horseradish peroxidase in the presence of hydrogen peroxide (HRP/H2O2) oxidizes a carcinogenic non-aminoazo dye, 1-phenylazo-2-hydroxynaphthalene (Sudan I) to the ultimate carcinogen, which binds to calf thymus DNA. The principal product of Sudan I oxidation by the HRP/H2O2 system is the benzenediazonium ion. Minor products are hydroxy derivatives of Sudan I, in which the aromatic rings are hydroxylated. The principal oxidative product (the benzenediazonium ion) is responsible for the carcinogenicity of Sudan I, because this ion, formed from this azo dye, binds to DNA.
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