Journal
ANALYTICAL AND BIOANALYTICAL CHEMISTRY
Volume 394, Issue 5, Pages 1361-1373Publisher
SPRINGER HEIDELBERG
DOI: 10.1007/s00216-009-2765-1
Keywords
HPLC-BCD; Patulin-glutathione adducts; Glutathione-S-transferase inhibition; ESI(+)-MS/MS; Fragmentation reactions
Funding
- Dr. Heinrich Luftmann (University of Munster, Germany)
- Studienstiftung des Deutschen Volkes (Bonn, Germany)
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A novel method for the identification of glutathione/electrophile adducts that are inhibiting glutathione-S-transferase (GST) activity was developed and applied for the analysis of the mycotoxin patulin. The method is based on high-performance liquid chromatography (HPLC) coupled to a continuous-flow enzyme reactor serving as biochemical detector (BCD) in parallel to electrospray mass spectrometric detection (ESI-MS). This HPLC-BCD technique combines a separation step and the detection of the inhibition and is therefore ideally suited for the analysis of the activity of single patulin/glutathione adducts within a complex mixture of adducts. Two out of at least 15 detected patulin-glutathione adducts showed strong GST inhibition. In ESI-MS, the inhibitory active adducts were characterized by [M + H](+) ions with m/z 462.1138 and m/z 741.2011, respectively. They could be identified as a dihydropyranone adduct containing one molecule glutathione and a ketohexanoic acid bearing two glutathione molecules. OnlineAbstractFigure.
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