Peroxidase-mediated reaction of the carcinogenic non-aminoazo dye 1-phenylazo-2-hydroxynaphthalene with transfer ribonucleic acid
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články
PubMed
2208592
DOI
10.1093/carcin/11.10.1789
Knihovny.cz E-zdroje
- MeSH
- biotransformace MeSH
- DNA metabolismus MeSH
- inbrední kmeny potkanů MeSH
- jaterní mikrozomy metabolismus MeSH
- karcinogeny metabolismus MeSH
- kinetika MeSH
- koncentrace vodíkových iontů MeSH
- křenová peroxidasa metabolismus MeSH
- krysa rodu Rattus MeSH
- naftoly metabolismus MeSH
- radioizotopy uhlíku MeSH
- RNA transferová metabolismus MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- mužské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- 1-phenylazo-2-naphthol MeSH Prohlížeč
- DNA MeSH
- karcinogeny MeSH
- křenová peroxidasa MeSH
- naftoly MeSH
- radioizotopy uhlíku MeSH
- RNA transferová MeSH
Horseradish peroxidase in the presence of hydrogen peroxide has the ability to mediate the activation of carcinogenic 1-phenylazo-2-hydroxynaphthalene (Sudan I) to DNA- and transfer RNA (tRNA)-bound products in vitro. tRNA is more accessible for modification by the activated carcinogen studied. tRNA modified by activated Sudan I becomes colored and has an absorption maximum of approximately 480 nm. Binding of metabolite(s) to tRNA is inhibited by ascorbate, glutathione, Mg2+ ions and nitrosobenzene. The mechanism of these protections was shown to be different for the different agents. tRNA modified by activated Sudan I exhibits a significantly increased acceptance for L-methionine. Enzymatic hydrolysis of modified tRNA with subsequent separation of nucleosides by HPLC suggests that the covalent modification of tRNA originating from the formation of more than one adduct with the nucleosides in tRNA is the predominant interaction of the activated Sudan I with tRNA.
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