Visser T J, Klootwijk W, Docter R, Hennemann G
Acta Endocrinol (Copenh). 1977 Nov;86(3):449-56. doi: 10.1530/acta.0.0860449.
The inactivation of thyrotrophin releasing hormone (pGlu-His-Pro-NH2, TRH) and its deamidated analogue pGlu-His-Pro-OH (TRH-OH) in human and rat serum has been studied using specific radioimmunoassays. No difference was apparent between human and rat serum with regard to proteolytic activity towards TRH and TRH-OH. It was found that the inactivation of both peptides is a saturable process. The disappearance of TRH was clearly inhibited by TRH-OH, luteinizing hormone-releasing hormone and dithiothreitol. The suppressive action of these compounds was observed to be dependent on their concentration. Proline and EDTA showed little inhibiting activity. Proline amide and pyroglutamic acid left the reaction unaffected. In no single instance could any production of TRH-OH from TRH be demonstrated.
利用特异性放射免疫分析法，对促甲状腺激素释放激素（pGlu-His-Pro-NH2，TRH）及其脱酰胺类似物pGlu-His-Pro-OH（TRH-OH）在人和大鼠血清中的失活情况进行了研究。在对TRH和TRH-OH的蛋白水解活性方面，人血清和大鼠血清之间未发现明显差异。结果发现，两种肽的失活都是一个可饱和的过程。TRH-OH、促黄体生成素释放激素和二硫苏糖醇明显抑制了TRH的消失。观察到这些化合物的抑制作用取决于它们的浓度。脯氨酸和乙二胺四乙酸显示出很小的抑制活性。脯氨酰胺和焦谷氨酸对反应没有影响。在任何情况下都未证明能从TRH产生TRH-OH。
