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Heterogeneity of circulating TSH‐receptor antibodies in thyroid disease demonstrated directly by chromatography
Author(s) -
Worthington J.,
Byfield P. G. H.,
Hlmsworth R. L.
Publication year - 1991
Publication title -
clinical endocrinology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.055
H-Index - 147
eISSN - 1365-2265
pISSN - 0300-0664
DOI - 10.1111/j.1365-2265.1991.tb00285.x
Subject(s) - trab , receptor , antibody , endocrinology , chemistry , medicine , affinity chromatography , elution , graves' disease , chromatography , radioimmunoassay , iodine , high performance liquid chromatography , thyroid , biochemistry , biology , immunology , organic chemistry , enzyme
Summary The heterogeneity of circulating TSH‐receptor antibodies (TRAb) has been demonstrated directly by affinity chromatography on the dye Remazol Yellow‐GGL. The technique resolved these antibodies Into discrete peaks within the general serum Immunoglobulln background. Peaks were detected initially by a binding (radioreceptor) assay and then characterized by their ability to stimulate the uptake of iodine‐125 Into FRTL‐5 cells. Thirteen subjects with high serum levels of TRAb were studied. The two hypothyrold patients each produced a single peak of TRAb activity with no ability to stimulate uptake of iodine‐125 into cultured cells. The remaining 11 patients had Graves’ disease; their sera produced a range of elution profiles after chromatography with TRAb activity resolved Into as many as five peaks. Considerable differences were seen in the relative abilities of the resolved TRAb components to bind to receptors and to stimulate cellular uptake of Iodine‐125 both between and within individual samples. No two patients produced components which chromatographed in the same position on the gradients employed for elution from the dye