Aguirre A, Donnadieu M, Job J C
Endocrinologia, Inst. Proagro, Sucre, Bolivia.
Horm Metab Res. 1991 Jun;23(6):281-4. doi: 10.1055/s-2007-1003674.
This study of the human growth hormone binding protein (GHBP) was undertaken using several samples of hGH, extractive or recombinant, from different origins. They were labelled in identical conditions and assayed by gel chromatography after incubation with three human sera having different levels of binding activity. For each serum the binding activities of the five recombinant hormones were very close and significantly higher (P less than 0.005) then the binding activities of the 2 extractive hormones. A radioactive peak which appeared in the zone of high molecular weights was more important with extractive than with recombinant hormones (P less than 0.01). This peak increased with the ageing of the tracer and appeared even when the tracer was incubated in the absence of serum. Thus, it is for its main part not related to another binding protein but, more likely, to a polymerization of the hormone. These data point out the importance of accurate technical conditions to have a reproducible assay for GHBP and to interpret the results in studies of growth disturbances.
本研究使用了来自不同来源的几种提取或重组的人生长激素（hGH）样本，对人生长激素结合蛋白（GHBP）进行了研究。这些样本在相同条件下进行标记，并在与三种具有不同结合活性水平的人血清孵育后，通过凝胶色谱法进行测定。对于每种血清，五种重组激素的结合活性非常接近，且显著高于（P<0.005）两种提取激素的结合活性。在高分子量区域出现的一个放射性峰，提取激素比重组激素更为明显（P<0.01）。该峰随示踪剂老化而增加，即使示踪剂在无血清条件下孵育也会出现。因此，其主要部分与另一种结合蛋白无关，而更可能与激素的聚合有关。这些数据指出了准确的技术条件对于进行可重复的GHBP测定以及在生长障碍研究中解释结果的重要性。
