Abstract
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 language | English |
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Pages (from-to) | 269-78 |
Number of pages | 10 |
Journal | Clinica Chimica Acta |
Volume | 184 |
Issue number | 3 |
DOIs | |
Publication status | Published - 16 Oct 1989 |
Keywords
- Bile/enzymology
- Chromatography, Gel
- Glutathione Transferase/antagonists & inhibitors
- Humans
- Isoenzymes/isolation & purification
- Radioimmunoassay