Many thanks Jacob and Mark for your questions/suggestions. In response:
So what happened with the non-reducing gel? (If the DTT was fresh, there
should be no problem, but if not...)
The gel is very clear, it shows the same exact pattern as the reducing gels.
Both high and low MW fractions run
Hi,
I have a protein that shows high and low MW peaks on gel filtration (which run
at the same MW on SDS-PAGE). There is a slow equilibrium because rerunning the
individual peaks on gel filtration a couple days later shows both peaks. The
higher MW peak is ~2 orders of magnitude more
Do you have a reducing agent in your solutions? I.e., maybe you are
seeing disulfides?
JPK
On Tue, Apr 12, 2011 at 1:27 PM, Michael Kenneth Fenwick
m...@cornell.edu wrote:
Hi,
I have a protein that shows high and low MW peaks on gel filtration (which
run at the same MW on SDS-PAGE). There
Thanks for all your suggestions so far...as a quick reply to some:
You say the fractions are in equilibrium - how about keeping the oligomer
fraction each time and adding it to the subsequent preparation?
I did this once. The equilibrium is sort of a gift that keeps on giving, but
the problem
So what happened with the non-reducing gel? (If the DTT was fresh,
there should be no problem, but if not...)
JPK
On Tue, Apr 12, 2011 at 3:21 PM, Michael Kenneth Fenwick
m...@cornell.edu wrote:
Thanks for all your suggestions so far...as a quick reply to some:
You say the fractions are in
