Abstract

Serum binding of binedaline, a new antidepressant drug, was studied in vitro by equilibrium dialysis. The percent of binding in serum is high, 99.2%, and remains constant within the range of therapeutic concentrations; no saturation to the binding sites was seen. Investigations performed on isolated proteins with a wide range of concentrations showed one site with a high affinity constant (Ka=2 × 106 M−1) for α1-acid glycoprotein and two sites with a low affinity constant (Ka=3 × 106 M−1). for human serum albumin. Binding to lipoproteins was nonsaturable, with a total affinity constant of 1.25 × 105<nKa<2.79 × 106 M−1. Over the range of therapeutic concentrations, the ratio of binedaline concentrations in serum and red blood cells remained constant (1%) and was shown to be dependent on the free fraction of binedaline in serum.

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