BINDING OF CORTICOSTEROIDS BY PLASMA PROTEINS. IV. THE ELECTROPHORETIC DEMONSTRATION OF CORTICOSTEROID BINDING GLOBULIN12

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Abstract
The binding of cortisol-4-C14, corticosterone-4-C14, and progesterone-4-C14 by human serum proteins has been studied by continuous flow paper electrophoresis. Careful predialysis of the serum, the steroid, and the electrophoretic buffer has prevented elution artifacts. With barbital buffer, pH 8.8, the peak of corticosterone binding migrates more slowly than albumin and is present in the alpha globulin region. In acetate buffer, pH 5.2, the corticosteroid binding globulin moves anodally away from the albumin component. Binding studies conducted with progesterone-4-C14 have permitted the demonstration of binding both by the anodally moving binding protein and by albumin. The bound progesterone could be displaced off the anodally moving component onto the albumin peak by adding cortisol to the system.