Glutathione S-transferase in human bile

A F Howie, P C Hayes, I A Bouchier, J D Hayes, G J Beckett

    Research output: Contribution to journalArticlepeer-review

    14 Citations (Scopus)


    Glutathione S-transferase (GST) isoenzymes have been measured by specific radioimmunoassay in human bile samples. GST Mu was found in 50% of samples while GST Pi, GST B1 and GST B2 were present in all samples; GST Pi constituted the major isoenzyme identified. The findings of the radioimmunoassay were confirmed by a one-step purification of GST from bile, using affinity chromatography, followed by their identification using sodium dodecyl sulphate-polyacrylamide gel (SDS-PAGE). Inhibition studies showed that, at the concentrations of bile salts found in bile, GST Pi would have little or no enzymic activity. It is proposed that GST Pi acts as a carrier protein of toxic, non-substrate, ligands to remove as yet unidentified substances from biliary epithelial cells and prevent their reabsorption.

    Original languageEnglish
    Pages (from-to)269-78
    Number of pages10
    JournalClinica Chimica Acta
    Issue number3
    Publication statusPublished - 16 Oct 1989


    • Bile/enzymology
    • Chromatography, Gel
    • Glutathione Transferase/antagonists & inhibitors
    • Humans
    • Isoenzymes/isolation & purification
    • Radioimmunoassay


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