leaving proteins in acetone too long?

[molbio123]

Hello,

I recently got a protein sample of which I reduced & alkylated, and acetone precipitated to get the protein part of the sample (and remove any junk) by centrifuging the sample in the acetone at low temp. I saw a pellet at the bottom. Then, I proceeded to add trypsin into the sample as I usually do for protein digestion, not remembering that I should dump out the acetone. So, I accidentally added in trypsin INTO the acetone during this step and forgot to dump the acetone supernatent before I added it in. I then left the sample to digest overnight in this acetone+trypsin.

My question is, will anything have happened to the protein or peptide fragments (if any) from leaving this sample in acetone overnight? and how long can the protein stay in acetone? thanks.

[StevieWonder]

was it done in eppendorf tubes? Because a thing I could think of is, that your acetone has worked in on the tubes, so you will get some peaks from the material the eppendorf is made of.

Before loading on the LC it's necessary to get off all aceton or other solvents, so that wouldn't be a problem. But I don't know the stability of proteins in aceton