Abstract
When the tritiation method for C-terminal analysis is applied to glutathione the labelling of glutamic acid is evident in addition to that of the C-terminal amino acid. It is possible that glutathione, when treated with acetic anhydride in the pyridine medium, forms N-acetylglutathione. This product can cyclize to form the oxazolone ring which readily incorporates tritium in the presence of 3H 2O. The labelling of non C-terminal glutamic acid may occur in proteins or peptides due to the presence of glutathione which can form mixed disulfides with proteins or when glutamic acid is in intrachain position with the γ-glutamyl-peptide linkage because this structure is very similar to acetylglutathione.
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