TY - JOUR
T1 - Glutathione mutagenesis in Salmonella typhimurium TA100
T2 - Dependence on a single enzyme, γ-glutamyltranspeptidase
AU - Stark, Avishay Abraham
AU - Zeiger, Errol
AU - Pagano, Dennis A.
PY - 1987/3
Y1 - 1987/3
N2 - Glutathione was mutagenic in Salmonella typhimurium strain TA100 in the presence of purified mammalian γ-glutamyltranspeptidase. Glutathione disulfide, γ-glutamyl glutamic acid, and S-methyl-glutathione were not mutagenic under the same conditions. Glutathione-mediated, γ-glutamyltranspeptidase-dependent mutagenesis of TA100 cells was inhibited by serine-borate complex, a known γ-glutamyltranspeptidase inhibitor, and potentiated by glycylglycine, a known γ-glutamyltranspeptidase enhancer. It is concluded that this enzyme is necessary and sufficient to activate glutathione to a mutagen.
AB - Glutathione was mutagenic in Salmonella typhimurium strain TA100 in the presence of purified mammalian γ-glutamyltranspeptidase. Glutathione disulfide, γ-glutamyl glutamic acid, and S-methyl-glutathione were not mutagenic under the same conditions. Glutathione-mediated, γ-glutamyltranspeptidase-dependent mutagenesis of TA100 cells was inhibited by serine-borate complex, a known γ-glutamyltranspeptidase inhibitor, and potentiated by glycylglycine, a known γ-glutamyltranspeptidase enhancer. It is concluded that this enzyme is necessary and sufficient to activate glutathione to a mutagen.
KW - (Salmonella typhimurium)
KW - Glutathione
KW - Glycylglycine
KW - Serine-borate complex
KW - γ-Glutamyltranspeptidase
UR - http://www.scopus.com/inward/record.url?scp=0023096187&partnerID=8YFLogxK
U2 - 10.1016/0027-5107(87)90020-0
DO - 10.1016/0027-5107(87)90020-0
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AN - SCOPUS:0023096187
SN - 0027-5107
VL - 177
SP - 45
EP - 52
JO - Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis
JF - Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis
IS - 1
ER -