Peroxidase-activated carcinogenic azo dye Sudan I (Solvent Yellow 14) binds to guanosine in transfer ribonucleic acid
Language English Country Slovakia Media print
Document type Journal Article
PubMed
8529865
Knihovny.cz E-resources
- MeSH
- Coloring Agents metabolism MeSH
- Guanosine metabolism MeSH
- Carcinogens metabolism MeSH
- Rats MeSH
- Guanosine Monophosphate metabolism MeSH
- Naphthols metabolism MeSH
- Nucleotides metabolism MeSH
- Peroxidase metabolism MeSH
- Polyribonucleotides metabolism MeSH
- RNA, Transfer metabolism MeSH
- In Vitro Techniques MeSH
- Binding Sites MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- 1-phenylazo-2-naphthol MeSH Browser
- Coloring Agents MeSH
- Guanosine MeSH
- Carcinogens MeSH
- Guanosine Monophosphate MeSH
- Naphthols MeSH
- Nucleotides MeSH
- Peroxidase MeSH
- Polyribonucleotides MeSH
- RNA, Transfer MeSH
Peroxidase in the presence of hydrogen peroxide catalyzes in vitro the activation of the carcinogenic azo dye Sudan I (1-phenylazo-2-hydroxynaphthalen) to tRNA-, homopolyribonucleotide- and 5'-monophosphate nucleoside-bound products. tRNA, poly G and guanosine 5'-monophosphate modified by activated Sudan I become colored and have an absorption maximum of approx. 480 nm. Cochromatographic analysis of adducts obtained by a reaction with tRNA and guanosine 5'-monophosphate on a thin layer of cellulose showed that the major Sudan I-tRNA adduct was formed by a reaction of activated Sudan I with guanosine in tRNA. The radical mechanism of the binding of the Sudan I molecule, containing the whole azo aromatic system, to nucleic acids is discussed.
