Iitaka M, Tanikawa T, Sakatsume Y, Yanagisawa M, Hara Y, Ishii J
Acta Endocrinol (Copenh). 1986 Jun;112(2):197-203. doi: 10.1530/acta.0.1120197.
Abnormally negative values of thyrotropin binding inhibitor immunoglobulin (TBII) were found in the sera from a patient with Graves' disease. This was due to the presence of potent bovine TSH (bTSH) binding activity in the sera. This activity was demonstrated to be in immunoglobulin G (IgG) with a lambda light chain isotype, which was shown to have an affinity for bTSH with a Ka value of 3.5 X 10(10) M-1 and a maximum binding capacity of 1.1 X 10(-14) M/mg IgG. F(ab')2 fragments obtained through pepsin digestion from the patient's IgG retained bTSH binding activity. [125I] bTSH binding to this IgG was inhibited by the TSH receptor. The inhibition was not completely competitive, suggesting the presence of different binding sites for this IgG and the TSH receptor on the TSH molecule. This IgG, however, could not bind labelled human TSH (hTSH). Since neither TSH nor other pituitary derivatives had ever been given to the patient, this bTSH binding activity was considered to be due to a spuriously occurring anti-bTSH antibody.
