Glutathione S-transferase in human bile

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

doi:10.1016/0009-8981(89)90060-0

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 journal › Article › peer-review

15 Citations (Scopus)

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
Pages (from-to)	269-78
Number of pages	10
Journal	Clinica Chimica Acta
Volume	184
Issue number	3
DOIs	https://doi.org/10.1016/0009-8981(89)90060-0
Publication status	Published - 16 Oct 1989

Keywords

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

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10.1016/0009-8981(89)90060-0

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title = "Glutathione S-transferase in human bile",

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.",

keywords = "Bile/enzymology, Chromatography, Gel, Glutathione Transferase/antagonists \& inhibitors, Humans, Isoenzymes/isolation \& purification, Radioimmunoassay",

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year = "1989",

month = oct,

day = "16",

doi = "10.1016/0009-8981(89)90060-0",

language = "English",

volume = "184",

pages = "269--78",

journal = "Clinica Chimica Acta",

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}

TY - JOUR

T1 - Glutathione S-transferase in human bile

AU - Howie, A F

AU - Hayes, P C

AU - Bouchier, I A

AU - Hayes, J D

AU - Beckett, G J

PY - 1989/10/16

Y1 - 1989/10/16

N2 - 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.

AB - 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.

KW - Bile/enzymology

KW - Chromatography, Gel

KW - Glutathione Transferase/antagonists & inhibitors

KW - Humans

KW - Isoenzymes/isolation & purification

KW - Radioimmunoassay

U2 - 10.1016/0009-8981(89)90060-0

DO - 10.1016/0009-8981(89)90060-0

M3 - Article

C2 - 2611999

SN - 0009-8981

VL - 184

SP - 269

EP - 278

JO - Clinica Chimica Acta

JF - Clinica Chimica Acta

IS - 3

ER -

Glutathione S-transferase in human bile

Abstract

Keywords

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