Binding of Sulfadimethoxine to Isolated Human Blood Protein Fractions

The binding of sulfadimethoxine to selected human blood protein fractions and to fresh serum has been examined by means of a new equilibrium dialysis technique which minimizes experimental error and permits the evaluation of low-level binding. Certain alpha-globulin fractions, containing mixtures of proteins, were found to bind the drug. Scatchard analysis of the binding of sulfadimethoxine to fresh serum, calculated as though all of the binding is due to albumin, gives a different result from that obtained with isolated albumin. This may be a reflection of the contribution of the alpha-globulins to the overall binding of sulfadimethoxine in fresh serum. Although sulfadimethoxine is amphoteric, it did not bind to the alpha 1-acid glycoprotein. The drug behaves as an acidic compound when binding to the blood proteins.