Could lysate be removed detergent, such as NP-40 and TritonX-100, if we treat the lysate with acetone?
And how much i would lose the protein if i do this?
Thanks.
It depends on the toughness of your protein. Most of the time acetone is too harsh for proteins and it denatures them. Use dialysis or ultrafiltration instead.
If you have a test to check your protein functionality before and after acetone treatment you could try that of course, however I agree with Omar that acetone probably denatures your protein. If you do not have a functional testing available you could try CD-spectroscopy to see if the folding opens due to acetone.
Getting rid of NP-40 and TX100 with dialysis is tough if not impossible even though the Mw would suggest otherwise. Many detergents form micelles in aquaeous solutions making them considerably larger than the Mw alone would suggest. This is particularly good to know if you are testing your protein with in vitro cell assays downstream as the detergents may have a lethal effect on cells even at fairly low concentrations.
I would refer you to read Pierce's technical note on the matter.
http://wolfson.huji.ac.il/purification/PDF/detergents/PIERCE_DetergentRemoval.pdf
It's not so much the loss of protein, but the damage the acetone will do.
If you can give some more information about what your trying to do (protein of interest, what you'll do with it), I could probably offer a better solution.
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