Gregory H, Thomas C E, Young J A, Willshire I R, Garner A
ICI Pharmaceuticals Division, Macclesfield, U.K.
Regul Pept. 1988 Aug;22(3):217-26. doi: 10.1016/0167-0115(88)90034-1.
Progressive enzymic degradation of human urogastrone-epidermal growth factor (URO-EGF) has given a series of fragments shortened at the C-terminus leading to removal of 20% of the structure. These peptides have been evaluated for their ability to bind to polyclonal antiserum and to isolated membrane receptors, to stimulate thymidine uptake by fibroblasts and to inhibit gastric acid secretion in rats. The related molecule human transforming growth factor-alpha, was also assayed and showed similar potency to URO-EGF in all systems. Reduced binding to the receptors of the fragments was paralleled by reduction in both biological activities indicating that this portion of the molecule was concerned entirely with receptor binding. After removal of 11 amino acids from the C-terminus the residue peptide was a full agonist although higher concentrations were necessary.
人尿抑胃素-表皮生长因子（URO-EGF）的逐步酶促降解产生了一系列在C端缩短的片段，导致20%的结构被去除。已对这些肽与多克隆抗血清和分离的膜受体结合的能力、刺激成纤维细胞摄取胸苷的能力以及抑制大鼠胃酸分泌的能力进行了评估。还检测了相关分子人转化生长因子-α，其在所有系统中显示出与URO-EGF相似的效力。片段与受体的结合减少与两种生物学活性的降低平行，这表明分子的这一部分完全与受体结合有关。从C端去除11个氨基酸后，剩余的肽是一种完全激动剂，尽管需要更高的浓度。
