Abstract
A purification scheme was devised that resulted in the resolution of a number of basic glutathione S-transferases from rat liver, three of which contained two subunits of molecular mass 23500 Da (i.e. Yb monomers). These were identified as transferases D, C and A by their elution positions from CM-cellulose and their specific activities towards a variety of substrates. Hybridization, immunotitration and peptide 'mapping' experiments demonstrated that transferases D, C and A comprise Yb2Yb2, Yb1Yb2 and Yb1Yb1 subunits.
| Original language | English |
|---|---|
| Pages (from-to) | 625-33 |
| Number of pages | 9 |
| Journal | Biochemical Journal |
| Volume | 213 |
| Issue number | 3 |
| Publication status | Published - 1 Sept 1983 |
Keywords
- Amino Acids/analysis
- Animals
- Electrophoresis, Paper
- Glutathione Transferase/isolation & purification
- Isoenzymes/isolation & purification
- Liver/enzymology
- Macromolecular Substances
- Peptide Fragments/analysis
- Rats
- Substrate Specificity