Bile acid inhibition of basic and neutral glutathione S-transferases in rat liver

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

A purification scheme is described for the neutral glutathione S-transferases of rat liver. Discontinuous sodium dodecyl sulphate/polyacrylamide-gel electrophoresis revealed that one of these enzymes contains a previously unidentified subunit, which has a molecular mass of 23 000 Da and has been designated Yn. Bile acids inhibited the activity of all the basic and neutral transferases investigated, but marked differences in the effects of bile acids on individual enzymes were observed. The activity of each transferase was inhibited more by lithocholate 3-sulphate than by chenodeoxycholate, which in turn was more inhibitory than cholate. The enzymes that were most sensitive to cholate inhibition were not found to be as readily inhibited as other transferases by chenodeoxycholate or lithocholate 3-sulphate. Conversely, the activity of transferase AA was more resistant to cholate, chenodeoxycholate and lithocholate 3-sulphate inhibition than was any of the other enzymes studied.

Original languageEnglish
Pages (from-to)581-8
Number of pages8
JournalBiochemical Journal
Volume215
Issue number3
Publication statusPublished - 1 Dec 1983

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Cholates
Transferases
Glutathione Transferase
Bile Acids and Salts
Chenodeoxycholic Acid
Liver
Rats
Enzymes
Molecular mass
Electrophoresis
Sodium Dodecyl Sulfate
Purification
Polyacrylamide Gel Electrophoresis
sulfolithocholic acid

Keywords

  • Animals
  • Chenodeoxycholic Acid/pharmacology
  • Cholic Acid
  • Cholic Acids/pharmacology
  • Chromatography, DEAE-Cellulose
  • Chromatography, Gel
  • Electrophoresis, Polyacrylamide Gel
  • Glutathione Transferase/antagonists & inhibitors
  • Kinetics
  • Lithocholic Acid/analogs & derivatives
  • Liver/enzymology
  • Male
  • Rats
  • Rats, Inbred Strains

Cite this

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title = "Bile acid inhibition of basic and neutral glutathione S-transferases in rat liver",
abstract = "A purification scheme is described for the neutral glutathione S-transferases of rat liver. Discontinuous sodium dodecyl sulphate/polyacrylamide-gel electrophoresis revealed that one of these enzymes contains a previously unidentified subunit, which has a molecular mass of 23 000 Da and has been designated Yn. Bile acids inhibited the activity of all the basic and neutral transferases investigated, but marked differences in the effects of bile acids on individual enzymes were observed. The activity of each transferase was inhibited more by lithocholate 3-sulphate than by chenodeoxycholate, which in turn was more inhibitory than cholate. The enzymes that were most sensitive to cholate inhibition were not found to be as readily inhibited as other transferases by chenodeoxycholate or lithocholate 3-sulphate. Conversely, the activity of transferase AA was more resistant to cholate, chenodeoxycholate and lithocholate 3-sulphate inhibition than was any of the other enzymes studied.",
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author = "Hayes, {J D} and J Chalmers",
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Bile acid inhibition of basic and neutral glutathione S-transferases in rat liver. / Hayes, J D; Chalmers, J.

In: Biochemical Journal, Vol. 215, No. 3, 01.12.1983, p. 581-8.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Bile acid inhibition of basic and neutral glutathione S-transferases in rat liver

AU - Hayes, J D

AU - Chalmers, J

PY - 1983/12/1

Y1 - 1983/12/1

N2 - A purification scheme is described for the neutral glutathione S-transferases of rat liver. Discontinuous sodium dodecyl sulphate/polyacrylamide-gel electrophoresis revealed that one of these enzymes contains a previously unidentified subunit, which has a molecular mass of 23 000 Da and has been designated Yn. Bile acids inhibited the activity of all the basic and neutral transferases investigated, but marked differences in the effects of bile acids on individual enzymes were observed. The activity of each transferase was inhibited more by lithocholate 3-sulphate than by chenodeoxycholate, which in turn was more inhibitory than cholate. The enzymes that were most sensitive to cholate inhibition were not found to be as readily inhibited as other transferases by chenodeoxycholate or lithocholate 3-sulphate. Conversely, the activity of transferase AA was more resistant to cholate, chenodeoxycholate and lithocholate 3-sulphate inhibition than was any of the other enzymes studied.

AB - A purification scheme is described for the neutral glutathione S-transferases of rat liver. Discontinuous sodium dodecyl sulphate/polyacrylamide-gel electrophoresis revealed that one of these enzymes contains a previously unidentified subunit, which has a molecular mass of 23 000 Da and has been designated Yn. Bile acids inhibited the activity of all the basic and neutral transferases investigated, but marked differences in the effects of bile acids on individual enzymes were observed. The activity of each transferase was inhibited more by lithocholate 3-sulphate than by chenodeoxycholate, which in turn was more inhibitory than cholate. The enzymes that were most sensitive to cholate inhibition were not found to be as readily inhibited as other transferases by chenodeoxycholate or lithocholate 3-sulphate. Conversely, the activity of transferase AA was more resistant to cholate, chenodeoxycholate and lithocholate 3-sulphate inhibition than was any of the other enzymes studied.

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KW - Chenodeoxycholic Acid/pharmacology

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KW - Cholic Acids/pharmacology

KW - Chromatography, DEAE-Cellulose

KW - Chromatography, Gel

KW - Electrophoresis, Polyacrylamide Gel

KW - Glutathione Transferase/antagonists & inhibitors

KW - Kinetics

KW - Lithocholic Acid/analogs & derivatives

KW - Liver/enzymology

KW - Male

KW - Rats

KW - Rats, Inbred Strains

UR - https://www.ncbi.nlm.nih.gov/pubmed/6661185

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JO - Biochemical Journal

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