Abstract
The glutathione-binding protein of Mytilus edulis possesses only one tryptophan per polypeptide. Quenching of intrinsic fluorescence due to this residue was studied in the presence of glutathione S-transferase ligands; hematin, bilirubin, biliverdin, bromosulphophthalein, 1-anilino-8-naphthalene sulphonate, 1,2-dichloro-4-nitrobenzene, ethacrynic acid and sodium deoxycholate as well as in the presence of triethyltin bromide. K(d) values were estimated from these experiments and were found to be 38-310 μM. Based on non-denaturing electrophoresis, the protein was found to have a native molecular weight of 50 kDa. Taken together with previously reported subunit molecular weights in the region of 25 kDa, this indicates that this protein has a dimeric quaternary structure.
| Original language | British English |
|---|---|
| Pages (from-to) | 439-443 |
| Number of pages | 5 |
| Journal | Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology |
| Volume | 115 |
| Issue number | 4 |
| DOIs | |
| State | Published - 1996 |
Keywords
- binding
- detoxification
- fluorescence
- glutathione
- mussel
- Mytilus edulis
- transferase
- xenobiotic