We are working on puryfing some proteins. Currently we need to make an
experiment in which denatured proteins possesing reduced -SH groups
have to be refolded. It is recommended to use dialysis with glutathione
in two forms oxidised GSSG and reduced GSH in 10:1 molar relation.
Unfortunately we don't have oxidised form. Do you recommend to use DTNB
(5,5'-Dithio-bis(2-nitrobenzoic acid))instead? It has disulfide bond,
it is used for SH groups quantification. Reagents' details r here
Or maybe DTNB binds to Cys group irreversible even in the presence of
glutatione? Could you provide us this information?
We would appreciate your interest