Plant activation and its role in environmental mutagenesis and antimutagenesis.
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.
Plewa
M J
MJ
Institute for Environmental Studies, University of Illinois at Urbana-Champaign, 61801, USA.
Wagner
E D
ED
Stavreva
D A
DA
Gichner
T
T
D016587:Antimutagenic Agents / Q000494:pharmacology*; D001711:Biotransformation; D002478:Cells, Cultured; D004791:Enzyme Inhibitors / Q000494:pharmacology; D016296:Mutagenesis; D009152:Mutagenicity Tests; D009153:Mutagens / Q000378:metabolism* / Q000633:toxicity; D010544:Peroxidases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010655:Phenylenediamines / Q000378:metabolism* / Q000633:toxicity; D010947:Plants, Toxic; D012486:Salmonella typhimurium / Q000235:genetics / Q000378:metabolism; D014026:Nicotiana / Q000201:enzymology*
D016587:Antimutagenic Agents; D004791:Enzyme Inhibitors; D009153:Mutagens; D010655:Phenylenediamines; D010544:Peroxidases; C008381:3-phenylenediamine