So what will happen is the glucose that is free to move in that solution will now compete for that active side found on that enzyme, enzyme number one, and it will outcompete that glucose that is bound onto the beads. And so once that glucose replaces the glucose that was bounced, the beads, that protein that was initially bounced, the bead, will essentially move away from that bead and will continue moving down our column because now it contains the active side that is filled with that glucose. And in this manner, we can basically wait until it goes all the way to the bottom. We can open up our knob, and so that will essentially be collected into some type of beaker or some type of test tube, as shown in the following diagram. And so now, following our affinity chromatography method, we have this solution that is purely one protein, protein one, the protein that we wanted to isolate in the first place. So we see that this method is only useful if we know what specific molecule that protein actually binds to, and if we also know that the other proteins in that mixture don't bind to that specific molecule, as we saw in this particular case.