Interactions of two substrates (L-glutamine and ADP) and Mn2+ ions with glutamine synthetase from Escherichia coli have been studied by calorimetry and equilibrium dialysis techniques. In addition, the use of calorimetry for establishing separateness of binding sites of different enzyme ligands is considered. The thermodynamic parameters for the sequential and simultaneous binding of L-glutamine and ADP to the unadenylylated Mn-enzyme have been determined. Thermal saturation curves for the binding of L-glutamine to the enzyme in the presence and absence of ADP were obtained at pH 7.1 and 30 °C. With saturating ADP and without ADP present. AG' values for L-glutamine binding are -3.83 and 16, NO.

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