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- W2076077605 abstract "Previously we reported the purification of soluble γ-glutamyltransferases (GGTs) from radish cotyledon. Subcellular fractionation of radish cells revealed that soluble GGT is a vacuolar enzyme. Acivicin, a GGT inhibitor, mediated the in vivo catabolism inhibition of the glutathione S-conjugate generated from endogenous glutathione and exogenously supplied monochlorobimane. Thus soluble GGT is possibly involved in the catabolism of glutathione S-conjugates." @default.
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- W2076077605 date "2006-07-23" @default.
- W2076077605 modified "2023-10-11" @default.
- W2076077605 title "Subcellular Localization and Possible Functions of γ-Glutamyltransferase in the Radish (<i>Raphanus sativus</i>L.) Plant" @default.
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- W2076077605 doi "https://doi.org/10.1271/bbb.60027" @default.
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