Azo-Dye binding to proteins and detoxication of p. dimethylaminoazobenzene in mouse and hamster liver

✍ Scribed by Françoise Decloitre; Michèle Meunier

• Publisher: John Wiley and Sons
• Year: 1970
• Tongue: French
• Weight: 486 KB
• Volume: 6
• Category: Article
• ISSN: 0020-7136
• DOI: 10.1002/ijc.2910060319

✦ Synopsis

Abstract

We studied azodye binding to proteins, and at the same time azoreductase and NADPH‐cytochrome c reductase activities in the liver of IC and C3H mice and hamsters fed DAB over a long period. Sensitivity of C3H mice to the toxic effects of DAB and resistance of IC mice and hamsters were confirmed by histological examinations. After 2–3 weeks of DAB feeding, the amount of protein‐bound azo‐dyes was three times higher in C3H mice than in IC mice. For hamsters, limited azo‐dye binding to proteins increased gradually up to 6 weeks, then remained nearly constant. In control animals azoreductase activity was five times higher in IC mice than in C3H mice; activity of hamsters was intermediate. NADPH‐cytochrome c reductase activity was nearly the same in all three groups, and was in no way related to azoreductase activity. The sensitivity of C3H mice to the toxic effects of DAB could be explained by their weak azoreductase activity and high level of azodye binding to proteins. On the contrary, high azoreductase activity in IC mice would allow detoxication of DAB and prevent or delay its toxic effects. Resistance of hamsters could be linked to the small amount of protein‐bound azo‐dye; yet, it cannot be explained by their weak azoreductase activity and probably depends on other metabolic processes, which have been considered.