GSH problem

tmitch1 tmitch1 at orion.it.luc.edu
Tue May 19 12:36:04 EST 1998


Hello.  I was wondering if anyone has used a glutathione analog in which the sulfhydral group 
is blocked to elude bound GST-fusion proteins from a GSH-Sepharose Chromatography Column
(Pharmacia).  Reduced glutathione (GSH) is currently used, but it binds to our peptides
via two disulfide bonds to two cysteines in our target peptide.  DTT removes the GSH, but it 
produces the target peptide with reduced cysteine residues.  We suspect that the cysteines 
form a native disulfide bond in the absence of GSH and DTT.  Any suggestions?  Thanks for your
time.

Tracy Mitchell
Loyola University of Chicago
tmitch1 at orion.it.luc.edu



More information about the Proteins mailing list