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Purification of the human thyroid peroxidase and its identification as the microsomal antigen involved in autoimmune thyroid diseases
Author(s) -
Czarnocka Barbara,
Ruf Jean,
Ferrand Mireille,
Carayon Pierre,
Lissitzky Serge
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80446-4
Subject(s) - thyroid , thyroid peroxidase , peroxidase , antigen , microsome , identification (biology) , immunology , medicine , biochemistry , endocrinology , chemistry , biology , enzyme , botany
Human thyroid peroxidase (TPO) has been purified from thyroid microsomes by immunoaffinity chromatography using a monoclonal antibody (mAb) to TPO. The eluted material had a specific activity of 381 and exhibited a peak in the Soret region. The ratio of A 411 to A 280 ranged from 0.20 to 0.25. Upon SDS‐polyacrylamide gel electrophoresis, the purified enzyme gave two contiguous bands in the 100 kDa region. Further, it has been demonstrated that sera with anti‐microsomal autoantibodies from patients presenting Graves' or Hashimoto's thyroiditis diseases were able to bind to purified TPO and to inhibit in a dose‐dependent manner the mAb binding to purified TPO. This suggests that TPO is the thyroid antigen termed to date the microsomal antigen.