EMAIL THIS PAGE TO A FRIEND

Bioscience, biotechnology, and biochemistry

Subcellular localization and possible functions of gamma-glutamyltransferase in the radish (Raphanus sativus L.) plant.


PMID 16861818

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.

Related Materials

Product #

Image

Description

Molecular Formula

Add to Cart

69899
Monochlorobimane, suitable for fluorescence, ≥70.0% (HPCE)
C10H11ClN2O2