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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 g...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2006-07, Vol.70 (7), p.1790-1793
Main Authors: Nakano, Y.(Kyoto Univ. (Japan)), Okawa, S, Prieto, R, Sekiya, J
Format: Article
Language:English
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Summary: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.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.60027