Immunological Analysis of Abnormal Binding of Thyroid Hormone in the Gamma-Globulin

Abstract

In a patient with Hashimoto's disease, abnormal binding of thyroid hormone in the gamma-globulin region was demonstrated by paper and cellulose acetate electrophoresis using various buffers (Glycine-acetate, Veronal and Tris-maleate). There was no binding of l-DIT or l-Tyrosine in the gamma-globulin region. After absorption of the patient's serum with thyroglobulin prior to electrophoresis, binding of thyroid hormone was remarkably decreased. Treatment of the patient with Prednisolone caused gradually diminished binding in the gamma-globulin region accompanied by a decrease of anti-thyroid antibody.Abnormal binding of thyroid hormone in the gamma-globulin region was not demonstrated in rabbits having high antibody titers against native thyroglobulin, but abnormal hormone binding was observed in all rabbits immunized against thyroglobulin denatured by heat, acid and alkali treatment. No binding of l-DIT or l-Tyrosine in the gamma-globulin region was observed in these sera. From these findings, it seems that the denaturation of thyroglobulin seems to permit antibody formation more readily against the thyroxyl structure which may act as hapten.Rabbits immunized with heat-denatured thyroglobulin had antibody against both heated thyroglobulin and untreated thyroglobulin. The patient's serum had a precipitating reaction against mildly denatured thyroglobulin, but not against strongly denatured thyroglobulin. The relationship between the antibody causing abnormal binding in the gamma-globulin region and thyroglobulin antigen is discussed.