Binding Affinity of Purified Plasma Proteins for Phenethylbiguanide, an Oral Hypoglycemic Compound

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Abstract
A colorimetric method has been adapted to the quantitative determination of the oral hypoglycemic compound phenethylbiguanide. This method was useful in studying the binding affinity of purified bovine plasma albumin and gamma globulin for the hypoglycemic agent. Equilibrium dialysis studies, which measure the decrease in thermodynamic activity of the bound cation, reveal that there is no significant interaction between phenethylbiguanide and the two native proteins. Consequently, the two plasma proteins are assumed to exert no buffering action in controlling the plasma concentration of the drug. The adherence of phenethylbiguanide to Beer's Law indicates that the compound exists in the monomeric state in aqueous solution below 10-4 molar.

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