I am working with reductase that has a cysteine residue in the active site, the enzyme is very well expressed and extremely pure, but has no activity at all, I added DTT to the purification buffer and to enzymatic assay, but still no activity. In the original paper the group used 1.4 mM beta mercaptoethanol during purification , does it make a difference?

Can I reactivate my protein now by adding beta mercaptoethanol or should I repeat the purification procedure?

Thanks

Similar questions and discussions