Burgus R, Butcher M, Amoss M, Ling N, Monahan M, Rivier J, Fellows R, Blackwell R, Vale W, Guillemin R
Proc Natl Acad Sci U S A. 1972 Jan;69(1):278-82. doi: 10.1073/pnas.69.1.278.
The primary structure of ovine hypothalamic hypophysiotropic luteinizing hormone-releasing factor, LRF, has been established as pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH(2) by hydrolysis of the peptide with chymotrypsin or pyrrolidone-carboxylylpeptidase and by analysis of the products by an Edman-dansylation sequencing technique, as well as by mass spectrometry of the derived phenylthiohydantoins. A decapeptide with the proposed primary structure, prepared by total synthesis, gave the same result on sequencing. The synthetic decapeptide possesses the same biological activities as the native ovine LRF. The amino-acid sequence of ovine LRF is identical to that already published for porcine LRF.
通过用胰凝乳蛋白酶或吡咯烷酮羧肽酶水解该肽，并采用埃德曼-丹磺酰化测序技术分析产物，以及对衍生的苯硫代乙内酰脲进行质谱分析，已确定绵羊下丘脑促垂体黄体生成素释放因子（LRF）的一级结构为pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH₂。通过全合成制备的具有所提出一级结构的十肽，测序结果相同。合成十肽具有与天然绵羊LRF相同的生物活性。绵羊LRF的氨基酸序列与已发表的猪LRF的氨基酸序列相同。
