Abstract
The conjugation products of E-destruxin (cyclodepsipeptide) with glutathione have been identified by fast-atom bombardment mass spectrometry. Appropriate conditions were developed for cyclodepsipeptide substrate, which enabled the direct, dynamic mass spectra analysis of spontaneous as well as glutathione-s-transferase catalyzed conjugation reactions. Application to the most active cyclopeptide in the series of destruxins yielded glutathionyl adduct.
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