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The IgG subclass distribution of thyroid autoantibodies
There have been several conflicting reports concerning the subclass distribution of thyroid autoantibodies. We have therefore reinvestigated this with both a radioimmunoassay and an ELISA based on the use of a variety of monoclonal antibodies. Our results demonstrate the presence of subclasses IgG1, IgG2, IgG3 and IgG4 in both thyroglobulin and microsomal autoantibodies from patients with either Graves' disease or Hashimoto's thyroiditis. However, in many patients there is over-representation of the IgG4 subclass. We also found marked differences in the binding characteristics of monoclonal antibodies directed against the same subclasses, underlining the need for appropriate selection of such monoclonal reagents in any assay.
There have been several conflicting reports concerning the subclass distribution of thyroid autoantibodies. We have therefore reinvestigated this with both a radioimmunoassay and an ELISA based on the use of a variety of monoclonal antibodies. Our results demonstrate the presence of subclasses IgG1, IgG2, IgG3 and IgG4 in both thyroglobulin and microsomal autoantibodies from patients with either Graves' disease or Hashimoto's thyroiditis. However, in many patients there is over-representation of the IgG4 subclass. We also found marked differences in the binding characteristics of monoclonal antibodies directed against the same subclasses, underlining the need for appropriate selection of such monoclonal reagents in any assay.
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Antibody Structure
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
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The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
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