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[PubMed] [Google Scholar] [87].Hudson V Rethinking cystic fibrosis pathology: the critical role of abnormal reduced glutathione (GSH) transport caused by CFTR mutation

In humans, GST often consists of two identical dimer subunits, with each subunit consisting of 210 amino acids and two binding sites, the G-site and the H-site (Figure 1)

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The isothiocyanates produced from the breakdown of glucosinolates by the action of the enzyme myrosinase [95] are highly electrophilic, a property of a compound that makes it readily available for the nucleophilic GSH when in the presence of GST [96]