Hi Francis,
I might save you some time by telling you up front you should just go
back and purify your compound to remove the impurity, you dont even
need to read the rest of this, just go.
Along the lines of what Savvas was saying, with any equilibrium
binding assay between two direct co
Hi Francis
I guess it depends on how much residual high-affinity binder you have in the
mixture and what the difference in affinity is between Y and deriv-Y. Another
issue is of course whether Y and derY compete for the same binding site and
have the same stoichiometry. A well designed displacem
Hi,
If your are talking about proteins or protein subunits, this means that you are
making polymers of nY, and Y becames the monomer. So in this case, I will not
consider Y as an impurity.
If I get you right, then size exclusion chromtography is good option to
separate the monomers from the
