Human thyroid peroxidase: autoantibody recognition depends on the natural conformation
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Updated: Nov 8, 2026

Generation of a Mouse Spontaneous Autoimmune Thyroiditis Model
Published on: March 17, 2023
H Berthold1, U Steffens, W Northemann
1Department of Molecular Biology, ELIAS Entwicklungslabor, Freiburg, Germany.
Abstract:
Thyroid peroxidase (TPO) purified from human thyroid glands was used to study the correlation relation between natural conformation and its ability for binding of autoantibodies in sera from patients with autoimmune lymphocytic thyroiditis (Hashimoto's thyroiditis). Treatment with heat (60 degrees C), urea, sodium dodecylsulfate (SDS), and dithiothreitol (DTT) decreased the autoantigenicity of TPO on average by 73.3%, 74.1%, 86.3%, and 91.8% measured by enzyme-linked immunosorbent assay (ELISA), respectively. These data demonstrate, that the binding of the majority of autoantibodies to human TPO depends on its natural conformation and modification.
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