Open AccessIodine induced alteration in immunological and biochemical properties of thyroglobulin.
Author(s) -
Andrzej Gardas,
Hanna Domek
Publication year - 1993
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.1993_4824
Subject(s) - iodine , thyroglobulin , iodide , chemistry , dithiothreitol , epitope , halogenation , biochemistry , cleavage (geology) , peptide , thyroid , endocrinology , antibody , organic chemistry , enzyme , immunology , biology , paleontology , fracture (geology)
The influence of iodine-iodide solution on the biochemical and immunological properties of human thyroglobulin (hTg) were studied. Human Tg preincubated with the iodine-iodide solution is split to small molecular mass fragments after disulphide bridge reduction with dithiothreitol. The peptide bond cleavage by iodine pretreatment and reduction is possibly linked with the coupling reaction of diiodotyrosyl residues. Pretreatment of hTg with iodine-iodide solution at 1-10 microM decreased the binding of autoantibodies to hTg. The iodine-iodide induced inactivation of hTg autoepitopes is pH dependent and is possibly caused by iodination of tyrosyl residues present in the epitope structure.