Inhibition of human glutathione S-transferases by bile acids.

@article{Singh1988InhibitionOH,
  title={Inhibition of human glutathione S-transferases by bile acids.},
  author={Shivendra V Singh and Teresinha Leal and Yogesh C. Awasthi},
  journal={Toxicology and applied pharmacology},
  year={1988},
  volume={95 2},
  pages={248-54}
}
Glutathione S-transferase (GST) isoenzymes isolated from various human tissues are differentially inhibited by bile acids. Trihydroxy bile acid (lithocholate) was found to be more inhibitory to all the human GST isoenzymes tested in this study, as compared to the monohydroxy (cholate) and dihydroxy (chenodeoxycholate) bile acids. Among the three major classes of GST, mu class isoenzymes are generally inhibited to a greater extent than the alpha and pi class isoenzymes. The results of this study… CONTINUE READING