Plenty of possible reasons for this :) But then, you're not telling us several important pieces of data - e.g. what else was in there with the protein, how the protein was concentrated, what was the protein theoretical pI, what was the protein size, was there *any* amount of protein that actually bound to the column - or did it *all* go through, what column material did you use, etc.
 
Without these data all we can offer is mostly speculation.
 
Three possibilities likely:
 
1. you had unexpected co-solute together with the protein and it prevented the binding
2. your pI was not right even at pH 8.0
3. your protein state changes with concentration (monomeric vs aggregated or oligomerized)
 
Tell us more details and maybe someone will have a more detailed explanation for you :)
 
Artem Evdokimov
----- Original Message -----
Sent: Monday, October 24, 2005 2:07 AM
Subject: [ccp4bb]: weird protein behavior during ion exhange chromatography

Hi
 
My protein of around 15mg/ml (0.3mM) was loaded to anion exchange column with 25mM Tris.HCl, pH8.0, but it came out before the gradient started, never sticking to the column. After I did the dilution by 10 to 15 fold, it showed to bind to the column.Anybody has the similar experience and share some explanations?
 
Thanks,
 
Capricy


Yahoo! FareChase - Search multiple travel sites in one click.

Reply via email to