Specific binding of thyroid-stimulating hormone by human serum globulins.
Specific binding of thyroid-stimulating hormone by human serum globulins.
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人血清球蛋白与促甲状腺激素的特异性结合。
DOI：
10.1677/joe.0.0880339
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发表时间：
1981
期刊：
影响因子：
--
通讯作者：
J. Biró
中科院分区：
文献类型：
--
作者：
J. Biró
对来自Graves病患者（甲状腺刺激免疫球蛋白（TSI）阳性）和12名健康人（TSI阴性）的球蛋白制剂（41份）进行了特异性促甲状腺激素（TSH）结合特性检测。两组球蛋白均具有131 I标记TSH的结合位点。TSI阴性对照组的平均解离常数（Kd）为6.8 pmol/1/mg球蛋白，最大特异性结合（Bmax）为3.0 pmol/mg球蛋白/1。二十四来自TSI阳性组的58.5%的球蛋白制剂具有相似的TSH结合特性，平均Kd为7.2 pmol/l/mg球蛋白，Bmax为3.6 pmol/mg球蛋白/l。（A型结合），但其余17个（41.5%）以不同方式结合TSH，Kd为71.5 pmol/l/mg球蛋白，Bmax为13.6 pmol/mg球蛋白/l（B型结合）。两种类型的特异性TSH结合在孵育1小时内达到最大水平，并具有最佳pH值7- 8。TSH结合量与球蛋白含量呈线性相关。这两种类型的结合是可逆的，通过添加过量的TSH和促性腺激素，促肾上腺皮质激素，催乳素和胰岛素竞争TSH的结合位点时，只有在相对较高的浓度。结合位点与大分子相关，它们在Sephadex G-200上层析后随空隙体积出现，并在纸电泳上随免疫球蛋白G（IgG）迁移。通过与抗人IgG的抗血清或人甲状腺膜预孵育，可降低球蛋白制剂的结合能力。
Globulin preparations (41) from patients with Graves's disease (positive to thyroid stimulating immunoglobulins; TSI) and 12 from healthy persons (TSI-negative) were tested for their specific thyrotrophin (TSH)-binding properties. Globulins from both groups possessed binding sites for 131I-labelled TSH. The mean dissociation constant (Kd) was 6.8 pmol/1 per mg globulin and the maximum specific binding (Bmax) was 3.0 pmol/mg globulin per 1 for the TSI-negative control group. Twenty-four (58.5%) globulin preparations from the TSI-positive group had similar TSH-binding characteristics with mean Kd of 7.2 pmol/1 per mg globulin and Bmax of 3.6 pmol/mg globulin per 1 (A-type binding) but the remaining 17 (41.5%) bound TSH in a different fashion with Kd of 71.5 pmol/1 per mg globulin and Bmax of 13.6 pmol/mg globulin per 1 (B-type binding). Both types of specific TSH binding reached the maximal level within 1 h of incubation and had an optimum pH of 7--8. There was a linear correlation between the amount of bound TSH and the globulin content of the samples. Both types of binding were reversible by the addition of an excess of TSH and gonadotrophins, ACTH, prolactin and insulin competed with TSH for the binding sites only when in relatively high concentrations. The binding sites were associated with macromolecules; they emerged with the void volume after chromatography on Sephadex G-200 and migrated with immunoglobulin G (IgG) on paper electrophoresis. The binding capacity of the globulin preparations could be decreased by preincubation with antiserum to human IgG or with human thyroid membranes.