Bulant M, Ladram A, Montagne J J, Delfour A, Nicolas P
Laboratoire de Bioactivation des Peptides, Institut Jacques Monod, Université Paris 7, France.
Biochem Biophys Res Commun. 1992 Dec 15;189(2):1110-8. doi: 10.1016/0006-291x(92)92319-s.
A neuropeptide termed TRH-potentiating peptide, which potentiates TRH-evoked thyrotropin secretion by antehypophysis in vitro, was isolated from an acetonic powder of bovine hypothalamus. The peptide was purified to homogeneity by a 3-step protocol involving molecular sieve filtration, ion-exchange chromatography and reverse phase high performance liquid chromatography. The complete amino acid sequence of the decapeptide was determined as Ser-Phe-Pro-Trp-Met-Glu-Ser-Asp-Val-Thr by automated Edman degradation with a solid-phase sequencer. Bovine TRH-potentiating peptide is structurally identical to Ps4, a decapeptide which was deduced from the cDNA encoding the rat TRH precursor. This study provides for the first time a direct chemical evidence for the existence of non-TRH peptides originating from posttranslational processing of the TRH precursor in vivo.
从牛下丘脑的丙酮粉中分离出一种名为促甲状腺激素释放激素（TRH）增强肽的神经肽，它在体外可增强TRH诱发的垂体前叶促甲状腺激素分泌。该肽通过包括分子筛过滤、离子交换色谱和反相高效液相色谱在内的三步方案纯化至同质。通过使用固相测序仪的自动埃德曼降解法确定该十肽的完整氨基酸序列为Ser-Phe-Pro-Trp-Met-Glu-Ser-Asp-Val-Thr。牛TRH增强肽在结构上与Ps4相同，Ps4是一种从编码大鼠TRH前体的cDNA推导出来的十肽。本研究首次提供了体内存在源自TRH前体翻译后加工的非TRH肽的直接化学证据。
