Subcellular Localization and Possible Functions of γ-Glutamyltransferase in the Radish (Raphanus sativus L.) Plant
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 <I>in vivo</I> catabolism inhibition of the glutathione <I>S</I>-conjugate generated from endogenous glutathione and exogenously supplied monochlorobimane. Thus soluble GGT is possibly involved in the catabolism of glutathione <I>S</I>-conjugates.
- Bioscience, biotechnology, and biochemistry
Bioscience, biotechnology, and biochemistry 70(7), 1790-1793, 2006-07-23
Japan Society for Bioscience, Biotechnology, and Agrochemistry