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THYROID HORMONE BINDING TO PUTATIVE NUCLEAR RECEPTORS IN HUMAN MONONUCLEAR BLOOD CELLS
Author(s) -
Maberly GF,
Eastman CJ,
Smith HC,
Waite K,
Wilke TJ
Publication year - 1982
Publication title -
australian journal of experimental biology and medical science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0004-945X
DOI - 10.1038/icb.1982.10
Subject(s) - peripheral blood mononuclear cell , triiodothyronine , receptor , nuclear receptor , hormone , thyroid hormone receptor , endocrinology , medicine , thyroid , cell , affinities , chemistry , biology , microbiology and biotechnology , in vitro , biochemistry , gene , transcription factor
Summary Nuclear protein extracts from mononuclear cells in normal subjects, subjects with the clinical syndrome of thyroid hormone resistance and cultured B lymphocytes bound thyroxine (T 4 ) (Ka; 1·3–3·5 × 10 9 m −1 ) and triiodothyronine (T 3 ) (Ka; 1·2–3·9 × 10 9 m −1 ) with similar affinities. When an extra wash step was introduced, the maximum specific binding of T 4 and T 3 was reduced by 75% and binding was abolished by three washes. These data suggest binding is to a serum protein contaminant present in the mononuclear cell preparation.