Human thyroid peroxidase: Autoantibody recognition depends on the natural conformation

Thyroid peroxidase (TPO) purified from human thyroid glands was used to study the correlation 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°C), urea, sod...

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Veröffentlicht in:Journal of clinical laboratory analysis 1993, Vol.7 (6), p.401-404
Hauptverfasser: Berthold, Heike, Steffens, Ute, Northemann, Wolfgang
Format: Artikel
Sprache:eng
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Zusammenfassung:Thyroid peroxidase (TPO) purified from human thyroid glands was used to study the correlation 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°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. © 1993 Wiley‐Liss, Inc.
ISSN:0887-8013
1098-2825
DOI:10.1002/jcla.1860070615