Jacob,
One of the problems with glutaraldehyde is the its chemistry is so
bizarre. It actually forms quite long transient polymers in
solution. You also have to ask yourself why formaldehyde also "fixes"
tissues. This is why glutaraldehyde works so well for tissue fixation
for EM as op
Dear Jacob,
agree, it's a mess. From what I read, the glutataldehyde concentration should
be low (<0.01%) and the x-linked complex that you get should not occur in high
salt conditions (reasoning that 1.2M KCl would break the average complex
apart). Have seen papers where more selective zero le
>> Maybe one should do a gradient of
>> gluteraldehyde concentrations, then plot the deviation of the observed
>> cross-linked oligomerization from a theoretical null hypothesis?
>
> Right - just do it side-by-side with a protein known to be monomeric of
> roughly the same size/lysine content... A
On Thu, 2011-09-15 at 15:10 -0500, Jacob Keller wrote:
> Maybe one should do a gradient of
> gluteraldehyde concentrations, then plot the deviation of the observed
> cross-linked oligomerization from a theoretical null hypothesis?
Right - just do it side-by-side with a protein known to be monomer
Dear Crystallographers and Biochemists,
cross-linking, say with gluteraldehyde, is an oft-used method of
demonstrating a protein's oligomeric state in solution. I have a
difficulty with this, however: theoretically (and in practice!), one
can tune the amount of cross-linker to get what ever result
