Subcellular localization and possible functions of gamma-glutamyltransferase in the radish (Raphanus sativus L.) plant.
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.
Nakano
Yoshihiro
Y
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
Okawa
Satoshi
S
Prieto
Rafael
R
Sekiya
Jiro
J
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*
D007555:Isoxazoles; D026901:Membrane Transport Proteins; D011720:Pyrazoles; C086860:glutathione transporter; C059597:monochlorobimane; D005723:gamma-Glutamyltransferase; D005978:Glutathione; C006303:acivicin