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. 1983 Dec 1;215(3):581–588. doi: 10.1042/bj2150581

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

J D Hayes, J Chalmers
PMCID: PMC1152439  PMID: 6661185

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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