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The Lactoperoxidase Method for Radiolabeling Protein

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

Abstract

This method, introduced by Marchalonis (1), employs lactoperoxidase in the presence of a trace of hydrogen peroxide to oxidize the radioactive iodide 125r to produce the reactive species 125I2 or 125I+. These reactive species substitute mainly into tyrosine residues of the protein, although substitution into other amino acid residues can occur under certain conditions. The oxidation can be stopped by simple dilution. Although the technique should result in less chance of denaturation of susceptible proteins than the chloramine T method, it is more technically demanding and is subject to a more marked variation in optimum reaction conditions.

Keywords

Amino Acid Residue Sodium Phosphate Buffer Sodium Azide Sodium Acetate Reactive Species 
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.

References

  1. 1.
    Marchalonis, J. J. (1969) An enzymic method for trace iodination of immunoglobulins and other proteins. Biochem. J. 113, 299–305.PubMedGoogle Scholar
  2. 2.
    Morrison, M. and Bayse, G. S. (1970) Catalysis of iodination by lactoperoxidase. Biochemistry 9, 2995–3000.PubMedCrossRefGoogle Scholar

Copyright information

© Humana Press Inc., Totowa, NJ 2002

Authors and Affiliations

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

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