Open AccessHuman thyroid peroxidase: Autoantibody recognition depends on the natural conformation
Author(s) -
Berthold Heike,
Steffens Ute,
Northemann Wolfgang
Publication year - 1993
Publication title -
journal of clinical laboratory analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 50
eISSN - 1098-2825
pISSN - 0887-8013
DOI - 10.1002/jcla.1860070615
Subject(s) - autoantibody , thyroid peroxidase , thyroid , peroxidase , natural (archaeology) , anti thyroid autoantibodies , medicine , immunology , computational biology , antibody , chemistry , biology , biochemistry , endocrinology , enzyme , paleontology
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.