I have 7mg of a 74kDa protein $A$ bound to a column. I want to bind another protein $B$ which is 19kDa onto protein $A$ so that every protein $A$ is bound (or as close to 100% binding as possible). I also know the $K_D$ of protein $A$ to protein $B$ is $9\cdot 10^{-8} M$, I am not sure if this is even relevant. How much of protein $B$ to I need to flow through to try to get complete binding?
One protein $A$ binds to one protein $B$. Can I just convert the 7mg into the amount that would result in one to one binding, i.e., 1.8mg of protein $B$? Then does the dissociation constant even matter? I don't have a ton of protein $B$ so I need to be frugal and calculate how much to use.