Piraphatdist T, Sugawa H, Inoue D, Enomoto T, Mori T, Imura H
2nd Division of Internal Medicine, Kyoto University, Faculty of Medicine, Japan.
Biochem Biophys Res Commun. 1990 Oct 30;172(2):529-36. doi: 10.1016/0006-291x(90)90705-r.
A synthetic decapeptide, P-194, which has the sequence No. 103 to 111 of hTSH receptor structure with an additional N-terminal tyrosine, did not bind TSH nor affected its receptor binding and thyroid stimulating activity. Preincubation of P-194 with sera from thyroid patients caused a significant decrease in TBII activity in almost all 12 TBII positive sera and an increase of thyroid stimulating activity in 3 of 7 Graves' IgG studied. In addition, [125I] P-194 bound to serum IgG fraction from thyroid patients with a positive correlation with TBII (N = 35, r = 0.509, p less than 0.01). The P-194 portion may be, at least a part of, TBII binding site distinct from the TSH binding site on the TSH receptor.
一种合成十肽P - 194,其具有hTSH受体结构的第103至111号序列,并在N端额外添加了酪氨酸,它既不结合TSH,也不影响其受体结合及甲状腺刺激活性。用甲状腺疾病患者的血清对P - 194进行预孵育,几乎使所有12份TBII阳性血清中的TBII活性显著降低,并且在所研究的7份格雷夫斯病IgG中的3份中甲状腺刺激活性增加。此外,[125I]P - 194与甲状腺疾病患者的血清IgG组分结合,与TBII呈正相关(N = 35,r = 0.509,p小于0.01)。P - 194部分可能至少是TSH受体上与TSH结合位点不同的TBII结合位点的一部分。