Abstract
Free thyroxine and thyroxine bound to thyroxine-binding globulin have been separated by gel nitration on polyacrylamide beads (Bio-gel). The elution patterns obtained are sufficiently consistent with the theoretical concept of saturation of the binding protein during the time employed for saturation assay of thyroxine. Standard curves of saturation assays of thyroxine are similar whether separation of bound and free hormone is achieved by gel filtration or if the free hormone is absorbed with anion exchange resin. Dissociation of the protein-thyroxine complex is too slow to have a significant effect on the resin separation system.
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