In article <4tjfb8$kjr at gwis2.circ.gwu.edu>,
mnrao at gwis2.circ.gwu.edu (Manjunath N.Rao) wrote:
->Hello Everyone,
->I am trying to remove triton X-100 from my protein solution. I have
->tried to remove it by dialysis. However, I dont think I have been able
->to remove it completely. I can tell this because of the foaming that
->occurs even after dialysis. I know that foaming is not due to my
protein
->because it is not a concentrated protein solution. Any help in this
->regard from any one of you out there is greatly appreciated.
Don't try to dialyse it - it has such a low CMC that could be
considered non-dialysable. Common methods for removing detergents:
1. Binding protein to a small column (DEAE, Q, Hydroxylapatite,
whatever you protein binds to), washing extensively and eluting
with appropriate solution w/o detergent.
2. Passing protein solution through lypophilic resin (like Bio-Rad's
Bio-Beads or smth.) Since this frequently results in protein binding,
Pierce has come up and is advertising an elegant solution: lypophylic
groups are inside beads only, with pore size smaller than most
proteins. Detegent binds, protein elutes in void (that's the same
principle as dialysis, but equals to > 100 dialysis changes).
It's called Extracti-Gel.
I have no idea as for how well it works and how inert toward
proteins it is. No affiliation with Pierce, etc. If you try it
and it works, please let me know - could be useful for many apps.
Good luck,
- Dima
