Enzymatic iodination of thyroglobulins obtained from patients with thyroid disease

• Published in: Nippon Naibunpi Gakkai zasshi Vol. 67; no. 10; p. 1186
• Main Authors: Tarutani, O, Yoshimura, H, Ohmori, T, Hosoya, T, Ishikita, T, Ishida, T
• Format: Journal Article
• Language: Japanese
• Published: Japan 20.10.1991
• Subjects: Antigen-Antibody Reactions; Humans; Iodide Peroxidase - metabolism; Iodine - metabolism; Lactoperoxidase - metabolism; Thyroglobulin - immunology; Thyroglobulin - metabolism; Thyroid Diseases - metabolism
• ISSN: 0029-0661
• DOI: 10.1507/endocrine1927.67.10_1186

Iodination of the isolated thyroglobulin (Tg) by peroxidase was compared with various Tg preparations obtained from patients with thyroid diseases. For the purpose, the iodination process was observed in the incubation medium containing Tg, iodide, H2O2-generating system, and thyroid peroxidase (TPO) or lactoperoxidase (LPO). During the incubation, iodination of Tg preparations increased gradually and reached a plateau after 90 min., and 5 min. incubation with 3mIU or 14mIU of TPO, respectively. The degree of iodination level at the plateau region was different in each Tg preparation, depending on the iodine content of the original starting (native) preparation before incubation. The iodination level of cancer Tg with a very low iodine content (less than 0.1%) was low compared with the normal Tg level (obtained from normal thyroid tissue which contained about 0.4% iodine). The above findings suggest the possible existence of some structural differences of Tg in terms of the susceptibility to the iodination between the preparations of normal and diseased Tgs. As far as the immunological aspect concerned, there was no significant difference in the affinity (avidity) of Tg with polyclonal anti-Tg antibody between the native Tg and the enzymatically iodinated one. These results suggest that the changes of iodine and thyroid hormone contents of Tg by in vitro iodination, has no significant effect on the immunological property of Tg molecule.