[Nature of the intracellular thyroid hormone receptor].
Thyroxine-binding proteins were isolated and purified by means of affine chromatography from the blood serum, 105 000 g of cytosol supernatant, non-histone protein fractions of chromatin, extracted with 0.4 M KCl. Identity of their molecular weights and of end aminoacids was found. A comparative study of proteins above, using chromatoelectrophoresis, has shown identity of their primary structure. The data obtained indicate, that chromatin and cytosol contain universal, thyroxine-binding protein, which structure is identical with that of prealbumin thyroxine-binding protein. This protein is considered to be a receptor, realizing the control of genome expression by thyroid hormones.
D000595:Amino Acid Sequence; D000818:Animals; D002467:Cell Nucleus / Q000032:analysis; D002843:Chromatin / Q000032:analysis; D003593:Cytoplasm / Q000032:analysis; D008099:Liver / Q000032:analysis; D011228:Prealbumin / Q000032:analysis*; D051381:Rats; D011956:Receptors, Cell Surface / Q000032:analysis*; D011988:Receptors, Thyroid Hormone; D012709:Serum Albumin / Q000032:analysis*; D013974:Thyroxine / Q000032:analysis*; D013975:Thyroxine-Binding Proteins / Q000032:analysis*
D002843:Chromatin; D011228:Prealbumin; D011956:Receptors, Cell Surface; D011988:Receptors, Thyroid Hormone; D012709:Serum Albumin; D013975:Thyroxine-Binding Proteins; D013974:Thyroxine
O prirode vnutrikletochnogo retseptora tireoidynkh gormonov.