title: Subcellular localization and possible functions of gamma-glutamyltransferase in the radish (Raphanus sativus L.) plant.
abstract: Previously we reported the purification of soluble gamma-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.
authors.affiliation: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Nakano
authors.forename: Satoshi
authors.initials: S
authors.lastname: Okawa
authors.forename: Rafael
authors.initials: R
authors.lastname: Prieto
authors.forename: Jiro
authors.initials: J
authors.lastname: Sekiya
mesh_terms: D005978:Glutathione / Q000378:metabolism; D007555:Isoxazoles / Q000494:pharmacology; D026901:Membrane Transport Proteins / Q000378:metabolism; D011720:Pyrazoles / Q000378:metabolism; D031224:Raphanus / Q000201:enzymology*; D014617:Vacuoles / Q000201:enzymology; D005723:gamma-Glutamyltransferase / Q000037:antagonists & inhibitors / Q000502:physiology*
chemical_list: D007555:Isoxazoles; D026901:Membrane Transport Proteins; D011720:Pyrazoles; C086860:glutathione transporter; C059597:monochlorobimane; D005723:gamma-Glutamyltransferase; D005978:Glutathione; C006303:acivicin