
pmid: 4197293
Abstract Binding capacities for thyroxine-binding globulin (TBG) and thyroxinebinding prealbumin (TBPA) and the equilibrium constants KTBg and Ktbpa were studied by competitive protein-binding techniques. A tracer dose of [ 125 I]thyroxine is equilibrated with the serum. Unlabelled thyroxine is added in concentrations from o to 200 μg/100 ml. Subsequent separation of free and bound hormone is carried out on Sephadex columns. These data are analysed by means of a Scatchard diagram with the bound/free hormone ratio as ordinate and the bound hormone as abscissa. The results agree with those obtained with other techniques. In our experience, this method is very useful for clinical evaluation.
Binding Sites, Temperature, Buffers, Hydrogen-Ion Concentration, Binding, Competitive, Salicylates, Evaluation Studies as Topic, Pregnancy, Iodine Isotopes, Phenytoin, Barbiturates, Freezing, Chromatography, Gel, Humans, Female, Serum Globulins, Dialysis, Mathematics, Serum Albumin, Protein Binding
Binding Sites, Temperature, Buffers, Hydrogen-Ion Concentration, Binding, Competitive, Salicylates, Evaluation Studies as Topic, Pregnancy, Iodine Isotopes, Phenytoin, Barbiturates, Freezing, Chromatography, Gel, Humans, Female, Serum Globulins, Dialysis, Mathematics, Serum Albumin, Protein Binding
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