I have a 19-mer peptide (2200 MW) with a C-terminal cysteine which I
purchased and received as a lyophilised powder. The company told me
that the peptide would be greater than 95% monomer, however the results
I have been getting would suggest that the majority of the peptide is
disulphide bonded. Is there any nice easy colorimetric reagent I can
use to detect free sulphydryl groups so that I can determine just how
much of my peptide is disulphide bonded? Alternatively does anybody
know a recipe for a gel that I could use to detect such a difference?
Thanks.
Mike Daws
