AI Article Synopsis
- - A new method using high-performance liquid chromatography (HPLC) and mass spectrometry was created to identify compounds that inhibit the enzyme glutathione-S-transferase (GST) by analyzing mycotoxin patulin and its adducts
- - This technique combines separation and detection, making it effective for studying individual patulin-glutathione adducts within a complex mix, leading to the discovery of at least 15 different adducts
- - Among these, two specific adducts were identified as strong inhibitors of GST, characterized by their unique molecular ion readings (m/z 462.1138 and m/z 741.2011) and associated with glutathione molecules.
Article Abstract
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.
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| http://dx.doi.org/10.1007/s00216-009-2765-1 | DOI Listing |
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