Science. 1989 Mar 17;243(4897):1481-3. doi: 10.1126/science.243.4897.1481.
A peptide that strongly stimulates the secretion of juvenile hormone from corpora allata in vitro (allatotropin) has been purified from extracts of heads of pharate adult Manduca sexta. The primary structure of this 13-residue peptide has been determined: H-Gly-Phe-Lys-Asn-Val-Glu-Met-Met-Thr-Ala-Arg-Gly-Phe-NH(2). This neurohormone has no sequence similarity with any known neuropeptide from other organisms. Synthetic allatotropin, as well as truncation fragments, including one with the five amino terminal residues deleted, showed in vitro activity indistinguishable from that of native allatotropin.
一种在体外强烈刺激咽侧体分泌保幼激素的肽（促前胸腺激素）已从处于预蛹期的成年烟青虫头部提取物中被纯化。这种由 13 个氨基酸残基组成的肽的一级结构已经确定：H-Gly-Phe-Lys-Asn-Val-Glu-Met-Met-Thr-Ala-Arg-Gly-Phe-NH(2)。这种神经激素与来自其他生物体的任何已知神经肽都没有序列相似性。合成的促前胸腺激素以及截断片段，包括缺失五个氨基末端残基的片段，在体外显示出与天然促前胸腺激素相同的活性。
