Stephenson F A, Bornstein J
Mol Cell Endocrinol. 1981 Aug;23(2):187-92. doi: 10.1016/0303-7207(81)90069-1.
The immunological reactivities of synthetic partial sequences of human growth hormone (hGH) and of an insulin-potentiating peptide isolated from human urine were studied using an antiserum raised against a synthetic hGH analogue [beta-Ala13]hGH(1-15). This antiserum contained antibodies directed mainly against a determinant in the sequence hGH(1-5). It was found that synthetic peptides containing the sequence Phe-Pro-Thr-Ile-Pro- (residues 1-5 of hGH) were immunologically active. Of the biologically active peptides studied, the synthetic peptide hGH(6-13) was virtually inactive and the urinary peptide was completely inert. Absence of immunologically detectable cross-reactivity lends support to the hypothesis that the amino acid sequence of urinary insulin-potentiating peptide (U-AcG) does not contain the hGH amino terminal sequence, Phe-Pro-Thr-Ile-Pro-.
使用针对合成的人生长激素（hGH）类似物[β-丙氨酸13]hGH(1 - 15)产生的抗血清，研究了人生长激素（hGH）的合成部分序列以及从人尿中分离出的一种胰岛素增强肽的免疫反应性。该抗血清含有主要针对hGH(1 - 5)序列中一个决定簇的抗体。发现含有序列苯丙氨酸-脯氨酸-苏氨酸-异亮氨酸-脯氨酸-（hGH的1 - 5位残基）的合成肽具有免疫活性。在所研究的生物活性肽中，合成肽hGH(6 - 13)几乎没有活性，而尿肽则完全无活性。免疫检测不到交叉反应性支持了这样的假说，即尿胰岛素增强肽（U - AcG）的氨基酸序列不包含hGH氨基末端序列苯丙氨酸-脯氨酸-苏氨酸-异亮氨酸-脯氨酸-。
