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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.

The mutual influence of ligand binding and self-association has been examined for phosphorylase b in the presence of a series of small ligands. The stepwise equilibrium constants describing the mutual dependence have been evaluated and discussed in terms of possible molecular mechanisms.

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