Abstract
A modified technique for zone electrophoresis in filter paper has been described, permitting the separation of a mixture in such a manner that the component with the slower electrophoretic mobility need not migrate in the path of the faster. Application of this reverse-flow technique to the study of thyroxine-binding by human serum proteins has overcome the artifacts due to adsorption of albumin-bound thyroxine in the globulin areas in conventional zone electrophoresis. An apparently reliable measurement of the thyroxine-binding capacity of the binding sites for thyroxine in the α-globulin has thus been obtained. In seven normal sera, this value ranged from 0.16 to 0.25 μg. thyroxine/ml. serum, with a mean of 0.19.
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