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A cyclic adenosine 3': 5'-monophosphate (Ado-3':5'-P) assay is proposed basing on the principle of competitive protein-binding. Free and bound Ado-3':5'-P is separatedjby coated (Dextran T 70, bovine serum albumine) charcoal. The Ado-3':5'-P binding protein is obtained from bull adrenals. The detection limit is 0.25 pmol in the incubation tube. The affinity constant of the protein-Ado-3': 5'-P complex is 2.8 · 10l/mol. The free enthalpy is approximate lOkcal/mol. The high specificity is tested with other similar nucleotides. There is a great difference between the N-monoand N-2'O-dibutyryl derivatives of Ado-3':5'-P with respect to their affinities for the binding protein, or protein kinase. The criteria of reliability are given by precision, detection limit, specificity and accuracy data. The method is suitable for serial determinations. One person is able to measure 100 samples (including the standard curve) per day. For linearisation of the dose response curve a new method is described. The proposed plot has the advantages of simplicity and ease of curve calculation. In addition, the plot yields the affinity constant and binding capacity of the binding protein. Moreover, this method allows the estimation of the affinity constant of any competitor of a labeled ligand. This method for linearisation is discussed regarding its limitations and advantages.

A Simple Competitive Protein-Binding Assay for Cyclic Adenosine 3´:5´-monophosphate