Purification and Assessment of Quality of Radioiodinated Protein

  • Graham S. Bailey
Part of the Springer Protocols Handbooks book series (SPH)


At the end of a radioiodination procedure, the reaction mixture will contain the labeled protein, unlabeled protein, radioiodide, mineral salts, enzyme (in the case of the lactoperoxidase method), and possibly some protein that has been damaged during the oxidation. For most uses of radioiodinated proteins, it is essential to have the labeled species as pure as possible. In theory, any of the many methods of purifying proteins can be employed (1). However, the purification of the radioiodinated protein should be achieved as rapidly as possible. For that purpose, the most widely used of all separation techniques is gel filtration.


Polyethylene Glycol Label Protein Specific Radioactivity Potassium Iodide Specific Antiserum 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


  1. 1.
    Harris, E. L. V. and Angal, S. (1989) Protein Purification Methods, IRL, Oxford, UK.Google Scholar
  2. 2.
    Welling, G. W. and Welling-Webster, S. (1989) Size-exclusion HPLC of proteins, in HPLC of Macromolecules (Oliver, R. W. A., ed.), IRL, Oxford, UK, pp. 77–89.Google Scholar
  3. 3.
    Desbuquois, B. and Aurbach, G. D. (1971) Use of polyethyleneglycol to separate free and antibody-bound peptide hormones in radioimmunoassays. J. Clin. Endocrin. Metab. 33, 732–738.CrossRefGoogle Scholar

Copyright information

© Humana Press Inc., Totowa, NJ 1996

Authors and Affiliations

  • Graham S. Bailey
    • 1
  1. 1.Department of Biological and Chemical SciencesUniversity of EssexColchesterUK

Personalised recommendations