Abstract
This paper reviews the use of in vitro and in vivo antimutagenicity studies that determined the role of plant peroxidases in the activation of arylamine promutagens. New information presented here suggests a model in which tobacco cell peroxidases exuded into the culture medium undergo a maturation process affecting their capacity to activate arylamine promutagens. Tobacco cell peroxidases are present in medium recovered from stationary phase cells and are associated with a fraction that sediments at 12000 x g. These peroxidases have a greater capacity to activate arylamines than do peroxidases present in the supernatant fluid. These data suggest that the plant activation of arylamines into products that are mutagenic in Salmonella typhimurium may be intimately involved in the process of lignification.
Original language | English (US) |
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Pages (from-to) | 163-171 |
Number of pages | 9 |
Journal | Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis |
Volume | 350 |
Issue number | 1 |
DOIs | |
State | Published - Feb 19 1996 |
Keywords
- Enzyme inhibition
- Peroxidase
- Promutagenic arylamine
- S. typhimurium YG1024
- Tobacco suspension cell
ASJC Scopus subject areas
- Molecular Biology
- Genetics
- Health, Toxicology and Mutagenesis