Stark A A, Zeiger E, Pagano D A
Mutat Res. 1987 Mar;177(1):45-52. doi: 10.1016/0027-5107(87)90020-0.
Glutathione was mutagenic in Salmonella typhimurium strain TA100 in the presence of purified mammalian gamma-glutamyltranspeptidase. Glutathione disulfide, gamma-glutamyl glutamic acid, and S-methyl-glutathione were not mutagenic under the same conditions. Glutathione-mediated, gamma-glutamyltranspeptidase-dependent mutagenesis of TA100 cells was inhibited by serine-borate complex, a known gamma-glutamyltranspeptidase inhibitor, and potentiated by glycylglycine, a known gamma-glutamyltranspeptidase enhancer. It is concluded that this enzyme is necessary and sufficient to activate glutathione to a mutagen.
在纯化的哺乳动物γ-谷氨酰转肽酶存在的情况下,谷胱甘肽在鼠伤寒沙门氏菌TA100菌株中具有致突变性。在相同条件下,谷胱甘肽二硫化物、γ-谷氨酰谷氨酸和S-甲基谷胱甘肽没有致突变性。TA100细胞的谷胱甘肽介导的、γ-谷氨酰转肽酶依赖性诱变被丝氨酸-硼酸盐复合物(一种已知的γ-谷氨酰转肽酶抑制剂)抑制,并被甘氨酰甘氨酸(一种已知的γ-谷氨酰转肽酶增强剂)增强。得出的结论是,这种酶对于将谷胱甘肽激活为诱变剂是必要且充分的。