The interactive binding of two ligands by an allosteric protein.
The equilibrium constants describing the simultaneous binding of the ligands AMP and 1-anilinonapthalene-8-sulfonate (ansyl) by phosphorylase b have been evaluated. The binding of a single molecule of AMP per dimer unit causes only a moderate reduction in the binding constant for a single molecule of ansyl, but reduces that for a second molecule of ansyl by 10-fold. The binding of two molecules of AMP per dimer unit almost abolishes the binding of a single molecule of ansyl.
D000249:Adenosine Monophosphate; D000494:Allosteric Regulation; D000495:Allosteric Site; D000817:Anilino Naphthalenesulfonates; D000818:Animals; D007700:Kinetics; D008024:Ligands; D046911:Macromolecular Substances; D008433:Mathematics; D009132:Muscles / Q000201:enzymology; D006005:Phosphorylases; D011485:Protein Binding; D011817:Rabbits
D000817:Anilino Naphthalenesulfonates; D008024:Ligands; D046911:Macromolecular Substances; D000249:Adenosine Monophosphate; D006005:Phosphorylases