Quality Control of Radioiodinated Products

  • Mrinal K. Dewanjee
Part of the Developments in Nuclear Medicine book series (DNUM, volume 21)


Structural alterations of labeled proteins and separation of free ligand have been studied by physicochemical properties such as electrophoretic mobility;[1] adsorption on hemoglobin-, dextran- , or plasma-coated charcoal;[2–4] cellulose powder, or silica;[5,6] and gel filtration. A rapid assessment of radioiodination damage to peptide hormones can be achieved by paper electrophoresis[1] (altered molecules have decreased mobility in the electrical field). Iodinated follicle stimulating hormone is not adsorbed on hemoglobin coated charcoal. In paper electrophoresis, the smaller anions (iodide, iodate, periodate) migrate rapidly toward the anode and run into the buffer. Short term electrophoresis is sufficient to separate these anions (Fig. 18–1).


Horseshoe Crab Metallic Silver Paper Electrophoresis Label Material Silver Bromide 
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Copyright information

© Springer Science+Business Media New York 1992

Authors and Affiliations

  • Mrinal K. Dewanjee
    • 1
    • 2
    • 3
  1. 1.Radiopharmaceutical LaboratoryUSA
  2. 2.Jackson Memorial Medical Center and University of Miami Hospital and ClinicsUSA
  3. 3.Surgery and Biomedical EngineeringUniversity of Miami School of MedicineUSA

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