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  • Title: Gamma-glutamylcysteine: a substrate for glutathione S-transferases.
    Author: Sugimoto M, Kuhlenkamp J, Ookhtens M, Aw TY, Reeve J, Kaplowitz N.
    Journal: Biochem Pharmacol; 1985 Oct 15; 34(20):3643-7. PubMed ID: 4052106.
    Abstract:
    A new high performance liquid chromatography (HPLC) method for the separation of gamma-glutamylcysteine (GC) from glutathione (GSH) following derivatization with 1-chloro-2,4-dinitrobenzene (CDNB) was developed using a Vydac C18 column and an acetonitrile-trifluoroacetic acid gradient. When the derivatization of GC, GSH, cysteine, and cysteinylglycine was performed with GSH S-transferase, peak heights for the GC and GSH derivatives were accentuated markedly, suggesting that GC, like GSH, is an enzyme substrate. Subsequently, GC was found to be a substrate for five purified forms of rat hepatic GSH S-transferase. However, the Km for GC was about 6-20 times higher than that for GSH. GSH was a competitive inhibitor of GC-CDNB conjugation, indicating that GC and GSH share the same binding site on the transferase. However, endogenous hepatic GC content in fed rats was only 5.8 +/- 0.1 nmoles/g, three orders of magnitude lower than GSH. Thus, under normal circumstances, GC would not be expected to contribute to detoxification reactions catalyzed by the GSH S-transferases. Its weak interaction with the GSH site of the GSH S-transferases supports the role of the glycine moiety of GSH in enhancing this interaction.
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