Identification and characterization of specific binding proteins for growth hormone in normal human sera.
Identification and characterization of specific binding proteins for growth hormone in normal human sera.
复制标题
正常人血清中生长激素特异性结合蛋白的鉴定和表征。
DOI：
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发表时间：
1986
影响因子：
15.9
通讯作者：
J. Stevenson
中科院分区：
文献类型：
--
作者：
A. Herington;S. Ymer;J. Stevenson
据报道，人血清中免疫反应性人生长激素（hGH）的公认“大”形式（45，000 - 100，000 mol wt）是无规聚集体或形式聚合物。然而，我们现在已经研究了它们是蛋白质结合形式的可能性。将单体125 I-hGH与正常血清孵育后，凝胶色谱显示结合125 I-hGH峰（约120，000 mol/wt），其完全被过量未标记hGH置换。当仅对血清进行色谱分析时，随后检测到两个特异性结合峰，在74，000和85，000 mol wt之间洗脱的主峰对应于在约120，000 mol wt处观察到的125 I-hGH结合蛋白复合物。使用用于分离结合激素与游离激素的微型凝胶过滤系统，正常人血清对125 I-hGH的结合依赖于时间（在21 ℃下2小时内达到平衡）、温度（21 ℃大于37 ℃）、Ca 2+和血清浓度。结合是可逆的，对hGH具有高度特异性，几个种属的GH或催乳素未显示。Scatchard分析显示亲和力（KA）为0.32 +/- 0.06 X 10（9）M-1（n = 7）的线性图。内源性hGH水平较低的人血清，当加入兔肝膜，以剂量依赖性的方式降低125 I-hGH在该组织中的结合。这些数据表明，人血清中含有一种特定的高亲和力hGH结合蛋白，这可能至少部分解释了血清中GH的已知大小异质性。其对GH与靶组织结合的影响可能表明结合蛋白在调节GH作用中的作用。
The well-recognized "big" forms (45,000-100,000 mol wt) of immunoreactive human growth hormone (hGH) in human serum have been reported to be random aggregates or formal polymers. However, we have now investigated the possibility that they are protein-bound forms. After incubation of monomeric 125I-hGH with normal serum, gel chromatography indicated a peak of bound 125I-hGH (at approximately 120,000 mol wt), which was completely displaced by excess unlabeled hGH. When serum alone was chromatographed two peaks of specific binding were subsequently detected, the major peak, eluting between 74,000 and 85,000 mol wt corresponded to the 125I-hGH-binding protein complex observed at approximately 120,000 mol wt. Using a mini-gel filtration system for separating bound from free hormone, binding of 125I-hGH by normal human serum was dependent on time (equilibrium was reached in 2 h at 21 degrees C), temperature (21 degrees C greater than 37 degrees C), Ca2+ and serum concentrations. Binding was reversible and highly specific for hGH, not being displayed by GH or prolactins from several species. Scatchard analysis revealed linear plots with an affinity (KA) of 0.32 +/- 0.06 X 10(9) M-1 (n = 7). Human serum with low endogenous hGH levels, when added to rabbit liver membranes, decreased the binding of 125I-hGH in this tissue in a dose-dependent manner. These data indicate that human sera contain a specific, high affinity binding protein for hGH and that this may account, at least in part, for the known size heterogeneity of GH in serum. Its effect on GH binding to target tissues may indicate a role for the binding protein in the regulation of GH action.
神经生长因子的生物合成及其作用机制。
DOI：
10.1016/b978-0-12-571137-1.50013-x
发表时间：
1981
期刊：
Recent progress in hormone research
影响因子：
--
作者：
Shooter,EM;Yankner,BA;Landreth,GE;Sutter,A
通讯作者：
Sutter,A
血小板衍生生长因子的血浆结合蛋白，抑制其与细胞表面受体的结合。
DOI：
10.1073/pnas.81.11.3424
发表时间：
1984
影响因子：
11.1
作者：
Raines,EW;Bowen-Pope,DF;Ross,R
通讯作者：
Ross,R