Glutathione S-transferase in human bile.
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.
Howie
A F
AF
University Department of Clinical Chemistry, Royal Infirmary, Edinburgh, Scotland, UK.
Hayes
P C
PC
Bouchier
I A
IA
Hayes
J D
JD
Beckett
G J
GJ
D001646:Bile / Q000201:enzymology*; D002850:Chromatography, Gel; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors / Q000145:classification / Q000302:isolation & purification*; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification*; D011863:Radioimmunoassay
D007527:Isoenzymes; D005982:Glutathione Transferase