In article <20040206003727.30725.qmail at ww02.hostica.com>,
<interpreneur_org at yahoo.com> wrote:
>In a binding or kinetic assay, how does the IC50 of a compound change
with respect to the number of receptors/enzyme molecules available? Is it
linear (e.g: 10 times more protein leads to a 10 fold increase in the
IC50)? Or not? And what is the mathematical equation explaining this?
Does the affinity/dissociation constant of the receptor/enzyme
change with the concentration of the receptor/enzyme? That is, as you add
more or less receptor/enzyme, does the binding energy between a receptor
molecule and an inhibitor molecule change?
Lou Hom >K'93
lhom at ocf.berkeley.eduhttp://www.ocf.berkeley.edu/~lhom/