I would guess that your GST tag is still bound to glutathione, as you suggest. 
Could you use a nickel column in your first purification step, instead of the 
glutathione sepharose? You might even be able to add your His-TEV onto the 
column for the proteolysis, then elute off the nickel column and put everything 
onto your glutathione sepharose.

Irit


On Jan 13, 2012, at 9:29 AM, Phelan, Paul J. wrote:

> I am trying to purify a protein, starting with a fusion that is double-tagged 
> with GST and poly-His, and my protein of interest also has an n-terminal 
> poly-His tag of its own.  So the fusion protein is 
> polyHis-GST-polyHis(Protein).  An initial step with glutathione Sepharose 
> works just fine, the fusion protein binds and is eluted with 10 mM 
> glutathione.  Digestion of the fusion protein (with His-tagged TEV protease) 
> also works, and gives me the polyHis-GST tag, plus polyHis(Protein).  BUT - 
> when I re-run the digested protein over glutathione Sepharose, the 
> polyHis-GST is not removed, and just passes through the column, along with 
> the polyHis(Protein).  Has anyone else seen a problem with GST from a 
> digested fusion protein not binding to glutathione Sepharose?  Could it be 
> that the GST still has glutathione tightly bound to it?  (The fusion protein 
> is digested by extensive dialysis with TEV protease).  Could it be that the 
> polyHis-GST is not behaving the same as non-tagged !
 GS!
> T?  This seems doubtful, since the fusion protein binds to glutathione 
> Sepharose in the first step.  Before anyone suggests using a Nickel resin to 
> remove the polyHis-GST, that's also a problem, since my protein of interest 
> (and also the TEV protease) is His-tagged too.
> 
> Any suggestions/insights would be welcome!
> 
> Paul Phelan
> Tufts University
> Boston
> 
> _______________________________________________
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> [email protected]
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