Insolubilized anithyroglobulin antibodies: properties and interest in the study of thyroglobulin

Abstract

Antithyroglobulin antibodies have been insolubilized, either through polymerization of the immune serum by ethyl chloroformate or through covalent binding to cyanogen bromide activated Sepharose 2B. These immunosorbents are able to bind thyroglobulin specifically, however, they have lost a part of the immune serum antibody activity. Thyroglobulin immunosorption is reversible. The degree of reversibility increases respectively with a pH 2 buffer, 3 M NaSCN and 0.1% sodium dodecylsulfate. After desorption by the first two procedures, thyroglobulin remains entirely precipitable by homologous antibodies, however, it undergoes conformational changes, some of them being partially reversible (unfolding of the 19S species, dissociation into 12S subunits). These immunosorbents may be used, under the conditions described, in the quantitative estimation and purification of thyroglobulin.