Value |
320
µM
Range: ±50 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 |
To evaluate product binding, equilibrium dialysis studies were
performed utilising GSDNB (1-S-glutathionyl-2,4-dinitrobenzene). When the data were fitted to a one site
binding hyperbola (Eq. (1) and Fig. 3), Bmax was determined to
3.6±0.3 product molecules per trimer, and Kd to 320±50µM. This
clearly shows three active-binding sites per trimer. Attempts to fit
data to a two or a three site-binding equation did not improve the
fit. |
Comments |
Researchers' results show that
three GSH molecules bind to each MGST1 trimer albeit with widely
varying affinities (20µM–2.5mM). The GSH molecule in the catalytically
competent thiolate anion form shows the highest affinity. A
complex product inhibition pattern supports subunit cooperativity
that is required for one-third-of-the-sites-reactivity. See BNID 105544, 105545, 105546 |
Entered by |
Uri M |
ID |
105547 |