Abstract
Cholic acid-binding activity in cytosol from rat livers appears to be mainly associated with enzymes having glutathione S-transferase activity; at least four of the enzymes in this group can bind the bile acid. Examination of the subunit compositions of different glutathione S-transferases indicated that cholic acid binding and the ability to conjugate reduced glutathione with 1,2-dichloro-4-nitrobenzene may be ascribed to different subunits.
| Original language | English |
|---|---|
| Pages (from-to) | 83-7 |
| Number of pages | 5 |
| Journal | Biochemical Journal |
| Volume | 185 |
| Issue number | 1 |
| Publication status | Published - 1 Jan 1980 |
Keywords
- Animals
- Cholic Acids/metabolism
- Chromatography, Ion Exchange
- Cytosol/enzymology
- Dinitrochlorobenzene/metabolism
- Electrophoresis, Polyacrylamide Gel
- Glutathione Transferase/isolation & purification
- In Vitro Techniques
- Isoenzymes/isolation & purification
- Liver/enzymology
- Rats
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