Electron microscopy of monoclonal antibody-linked chains of thyroglobulin molecules.
Negative staining electron microscopy visualized immune complexes of hog thyroglobulin produced by 3 monoclonal antibodies, each towards a different conformation-dependent antigenic structure of the thyroglobulin. Equimolar mixtures of the thyroglobulin and any one of the 3 antibodies formed peculiar unbranched chains of 'ovoid' thyroglobulin molecules linked by the antibody molecules in an 'end to end' fashion. A mixture of the thyroglobulin and the 2 different antibodies produced branched chains. A set of 3 conformation-dependent antigenic structures was thus located near each end of the elongated thyroglobulin molecule. The results also indicated a topological similarity between the 2 subunits of thyroglobulin.
Y
Y
Kondo
K
K
Inoue
E
E
Kondo
N
N
Ui
D000818:Animals; D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D000939:Epitopes; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D013552:Swine; D013954:Thyroglobulin / Q000276:immunology
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D000939:Epitopes; D046911:Macromolecular Substances; D013954:Thyroglobulin