In vitro enhancement of the mutagenicity of 4‐nitro‐o‐phenylenediamine by plant S‐9

James M. Gentile; Glenda J. Gentile; Steven Townsend; Michael J. Plewa

doi:10.1002/em.2860070104

In vitro enhancement of the mutagenicity of 4‐nitro‐o‐phenylenediamine by plant S‐9

James M. Gentile, Glenda J. Gentile, Steven Townsend, Michael J. Plewa

Crop Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

The direct‐acting mutagen 4‐nitro‐o‐phenylenediamine (NOP) was activated in vitro by pea or tobacco S‐9 into a more potent mutagen in Salmonella typhimurium strain TA98. NOP mutagenicity was not altered by Aroclor 1254‐induced rat liver S‐9. The plant S‐9 activation of NOP was heat‐sensitive but was not NADPH‐dependent, did not involve superoxide radicals, and was not inhibited by CO. A direct relationship between plant peroxidase and NOP activation was established. Several purified peroxidases including horseradish peroxidase, chloroperoxidase, and lactoperoxidase also activated NOP. The perodoxidative process was not H₂O₂‐dependent but was partially inhibited by a peroxidase inhibitor.

Original language	English (US)
Pages (from-to)	73-85
Number of pages	13
Journal	Environmental Mutagenesis
Volume	7
Issue number	1
DOIs	https://doi.org/10.1002/em.2860070104
State	Published - 1985

Keywords

4‐nitro‐o‐phenylenediamine
Salmonella
in vitro
peroxidase
plant activation

ASJC Scopus subject areas

Genetics
Health, Toxicology and Mutagenesis

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title = "In vitro enhancement of the mutagenicity of 4‐nitro‐o‐phenylenediamine by plant S‐9",

abstract = "The direct‐acting mutagen 4‐nitro‐o‐phenylenediamine (NOP) was activated in vitro by pea or tobacco S‐9 into a more potent mutagen in Salmonella typhimurium strain TA98. NOP mutagenicity was not altered by Aroclor 1254‐induced rat liver S‐9. The plant S‐9 activation of NOP was heat‐sensitive but was not NADPH‐dependent, did not involve superoxide radicals, and was not inhibited by CO. A direct relationship between plant peroxidase and NOP activation was established. Several purified peroxidases including horseradish peroxidase, chloroperoxidase, and lactoperoxidase also activated NOP. The perodoxidative process was not H2O2‐dependent but was partially inhibited by a peroxidase inhibitor.",

keywords = "4‐nitro‐o‐phenylenediamine, Salmonella, in vitro, peroxidase, plant activation",

author = "Gentile, {James M.} and Gentile, {Glenda J.} and Steven Townsend and Plewa, {Michael J.}",

year = "1985",

doi = "10.1002/em.2860070104",

language = "English (US)",

volume = "7",

pages = "73--85",

journal = "Environmental and Molecular Mutagenesis",

issn = "0893-6692",

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T1 - In vitro enhancement of the mutagenicity of 4‐nitro‐o‐phenylenediamine by plant S‐9

AU - Gentile, James M.

AU - Gentile, Glenda J.

AU - Townsend, Steven

AU - Plewa, Michael J.

PY - 1985

Y1 - 1985

N2 - The direct‐acting mutagen 4‐nitro‐o‐phenylenediamine (NOP) was activated in vitro by pea or tobacco S‐9 into a more potent mutagen in Salmonella typhimurium strain TA98. NOP mutagenicity was not altered by Aroclor 1254‐induced rat liver S‐9. The plant S‐9 activation of NOP was heat‐sensitive but was not NADPH‐dependent, did not involve superoxide radicals, and was not inhibited by CO. A direct relationship between plant peroxidase and NOP activation was established. Several purified peroxidases including horseradish peroxidase, chloroperoxidase, and lactoperoxidase also activated NOP. The perodoxidative process was not H2O2‐dependent but was partially inhibited by a peroxidase inhibitor.

AB - The direct‐acting mutagen 4‐nitro‐o‐phenylenediamine (NOP) was activated in vitro by pea or tobacco S‐9 into a more potent mutagen in Salmonella typhimurium strain TA98. NOP mutagenicity was not altered by Aroclor 1254‐induced rat liver S‐9. The plant S‐9 activation of NOP was heat‐sensitive but was not NADPH‐dependent, did not involve superoxide radicals, and was not inhibited by CO. A direct relationship between plant peroxidase and NOP activation was established. Several purified peroxidases including horseradish peroxidase, chloroperoxidase, and lactoperoxidase also activated NOP. The perodoxidative process was not H2O2‐dependent but was partially inhibited by a peroxidase inhibitor.

KW - 4‐nitro‐o‐phenylenediamine

KW - Salmonella

KW - in vitro

KW - peroxidase

KW - plant activation

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