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Levels of the tripeptide glutathione (GSH) and the activity of glutathione S-transferases were investigated in S9 fractions of rats and mice and in Salmonella typhymurium tester strains TA1535, TA100, TA1538 and TA98. The S9 and Salmonella typhimurium tester strains had high levels of glutathione. Compared with S9, the activity of GSH S-transferases was lower in the bacteria. However, electrophiles such as 1-chloro-2,4-dinitrobenzene (CDNB), diethyl maleate and styrene oxide were effectively bound to bacterial GSH. The mutagenicity of the direct mutagen CDNB was drastically lowered in presence of S9 fractions but not in presence of microsomes. A comparable decrease was obtained when microsomal supernatant, which contains GSH and GSH S-transferases, was added to the microsomes. Addition of GSH in excess completely abolished mutagenicity of CDNB. These results demonstrate that the conjugation of electrophiles with GSH mediated by the S9 fraction or the bacterial tester strains represents an important detoxication mechanism which may influence the results obtained with the Salmonella typhimurium mammalian-microsome mutagenicity test.
K H Summer, and
W Göggelmann, and
H Greim
November 1979,
Mutation research,
K H Summer, and
W Göggelmann, and
H Greim
December 1978,
Il Farmaco; edizione pratica,
K H Summer, and
W Göggelmann, and
H Greim
February 1980,
Veterinary and human toxicology,
K H Summer, and
W Göggelmann, and
H Greim
May 1979,
Mutation research,
K H Summer, and
W Göggelmann, and
H Greim
January 1988,
Mutation research,
K H Summer, and
W Göggelmann, and
H Greim
February 1987,
Mutation research,
K H Summer, and
W Göggelmann, and
H Greim
May 1987,
Mutation research,
K H Summer, and
W Göggelmann, and
H Greim
October 1983,
Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association,
K H Summer, and
W Göggelmann, and
H Greim
July 1983,
Mutation research,
K H Summer, and
W Göggelmann, and
H Greim
July 1979,
Cancer letters,
