Affinity of one GSH bound per Microsomal glutathione transferase 1 trimer
| Value | 16 µM Range: ±4 µM |
|---|---|
| Organism | Rat Rattus norvegicus |
| Reference | Alander et al., Microsomal glutathione transferase 1 exhibits one-third-of-the-sites-reactivity towards glutathione. Arch Biochem Biophys. 2009 Jul 1 487(1):42-8. p. 44 right column, 2nd paragraphPubMed ID19416719 |
| Method | In order to re-evaluate their previous binding data researchers repeated equilibrium dialysis experiments with 35S-labelled GSH as described in [Sun et al., 1997 PMID 9337868], with the exception that 10 mM b-mercaptoethanol was used as a reducing agent instead of 0.1 M DTT. With the enzyme concentration used (29–31µM trimer corresponding to ˜90µM potential binding sites), they could only observe one GSH bound per trimer (Bmax 0.85±0.03, Kd 16±4µM, Eq. (1) and Fig. 2), confirming their previous results [Sun et al., above]. |
| Comments | Researchers therefore suggest that MGST1 harbours one high affinity and two low affinity sites for GSH. MGST1 binds three GSH molecules per trimer. See BNID 105544, 105546, 105547 |
| Entered by | Uri M |
| ID | 105545 |