Abstract
The glutathione S-transferases are dimeric enzymes whose subunits can be defined by their mobility during sodium dodecyl sulphate/polyacrylamide-gel electrophoresis as Yf (Mr 24,500), Yk (Mr 25,000), Ya (Mr 25,500), Yn (Mr 26,500), Yb1 (Mr 27,000), Yb2 (Mr 27,000) and Yc (Mr 28,500) [Hayes (1986) Biochem. J. 233, 789-798]. Antisera were raised against each of these subunits and their specificities assessed by immuno-blotting. The transferases in extrahepatic tissues were purified by using, sequentially, S-hexylglutathione and glutathione affinity chromatography. Immune-blotting was employed to identify individual transferase polypeptides in the enzyme pools from various organs. The immuno-blots showed marked tissue-specific expression of transferase subunits. In contrast with other subunits, the Yk subunit showed poor affinity for S-hexylglutathione-Sepharose 6B in all tissues examined, and subsequent use of glutathione and glutathione affinity chromatography. Immuno-blotting was employed to identify a new cytosolic polypeptide, or polypeptides, immunochemically related to the Yk subunit but with an electrophoretic mobility similar to that of the Yc subunit; high concentrations of the new polypeptide(s) are present in colon, an organ that lacks Yc.
Original language | English |
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Pages (from-to) | 779-88 |
Number of pages | 10 |
Journal | Biochemical Journal |
Volume | 233 |
Issue number | 3 |
DOIs | |
Publication status | Published - 1 Feb 1986 |
Keywords
- Animals
- Chromatography, Affinity
- Cross Reactions
- Cytosol/metabolism
- Electrophoresis, Polyacrylamide Gel
- Glutathione Transferase/analysis
- Immunoglobulin G/immunology
- Isoenzymes/analysis
- Male
- Peptide Fragments/immunology
- Proteins/metabolism
- Rats
- Rats, Inbred Strains
- Tissue Distribution