Clinical Chemistry
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Clinical Chemistry 40: 442-447, 1994;
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Clinical Chemistry, Vol 40, 442-447, Copyright © 1994 by American Association for Clinical Chemistry

Microparticle-enhanced nephelometric immunoassay of anti-thyroid peroxidase autoantibodies in thyroid disorders

AA Harchali, P Montagne, J Ruf, ML Cuilliere, MC Bene, G Faure and J Duheille
Immunology Laboratory, Faculty of Medicine, Vandoeuvre, France.

Crude thyroid peroxidase extracted from human thyroid microsomes was covalently bound onto polyacrylic and polyfunctional copolymerized microparticles. We observed agglutination of the thyroid peroxidase- microparticle conjugate with 13 monoclonal antibodies (mAbs) specific for epitopes on four different antigenic domains of human thyroid peroxidase (TPO; EC 1.11.1.7), after addition of anti-mouse immunoglobulins. We quantified agglutination by measuring with a specially designed nephelometer the light scattered by the conjugates. This allowed us to develop a microparticle-enhanced nephelometric immunoassay for human anti-TPO autoantibodies (aAbs) with defined epitopic specificity, based on the ability of aAbs to inhibit mAb- induced agglutination. Applied to patients with autoimmune thyroid diseases, this assay confirmed the polyclonality of anti-TPO aAbs and their preferential reactivity toward epitopes located on the A and B antigenic domains of the TPO molecule. The same specificities seem to be present in patients with Hashimoto thyroiditis or Graves disease.


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A Conformational B-cell Epitope on the C-terminal End of the Extracellular Part of Human Thyroid Peroxidase
J. Biol. Chem., April 3, 1998; 273(14): 8056 - 8062.
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