a problem in protein purification

David Micklem drm21 at mole.bio.cam.ac.uk
Mon Nov 7 14:10:29 EST 1994

In article <39kpv8$nbf at lyra.csx.cam.ac.uk>, dh124 at cus.cam.ac.uk (D.
Hodges) wrote:
> I've eluted proteins from a monoclonal affinity column using 3M sodium 
> iodide (pH7.2) - fractions go staight into dialysis against a more protein
> friendly buffer as soon as they come off the column. It's worked very 
> for a small protein (30K) but you never know how anything else would
> behave - might be worth a try though.
> Debbie

I'll second that.  I used 2.5M sodium iodide to elute an antibody off an
affinity column one time when I couldn't use low pH.  After dialysis the
antibody worked just fine...

In Yuling's case, I don't know if it would work - the protein should
probably stay soluble in the NaI since its a denaturant, but I guess
there's a pretty good chance it'll come out of solution during dialysis -
maybe other people's suggestions will help with that.  Let us know what
worked if you manage to crack it!

Good luck, David

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