Piot J M, Zhao Q, Guillochon D, Ricart G, Thomas D
Laboratoire de Technologie des Substances Naturelles, Villeneuve D'Ascq, France.
Biochem Biophys Res Commun. 1992 Nov 30;189(1):101-10. doi: 10.1016/0006-291x(92)91531-t.
Two opioid peptides were isolated from a bovine hemoglobin hydrolysate, by use of gel permeation (GP) and reverse phase (RP) high performance liquid chromatography (HPLC). Their primary structure and accurate molecular weights, determined by amino acid analysis and fast atom bombardment (FAB) mass spectrometry, were identical to fragments 31-40 (LVV-hemorphin-7) and 32-40 (VV-hemorphin 7) of the beta-chain of bovine hemoglobin. The same fragments occur in human hemoglobin in positions 32-41 and 33-41 of the beta-chain, respectively. The opioid potency of these peptides, exhibited by use of electrically stimulated muscle of isolated guinea-pig ileum (GPI), were significant and comparable with some others previously described. In addition, the location of the two opioid peptides, VV-hemorphin-7 and LVV-hemorphin-7, revealed the existence of a "strategic zone" both in the bovine and human beta-chains of hemoglobin.
通过凝胶渗透（GP）和反相（RP）高效液相色谱（HPLC），从牛血红蛋白水解物中分离出两种阿片样肽。经氨基酸分析和快原子轰击（FAB）质谱法测定，它们的一级结构和精确分子量与牛血红蛋白β链的片段31 - 40（LVV - 血啡肽 - 7）和32 - 40（VV - 血啡肽7）相同。相同的片段分别出现在人血红蛋白β链的32 - 41位和33 - 41位。利用豚鼠离体回肠（GPI）的电刺激肌肉实验显示，这些肽的阿片样活性显著，且与之前描述的其他一些肽相当。此外，两种阿片样肽VV - 血啡肽 - 7和LVV - 血啡肽 - 7的位置揭示了在牛和人血红蛋白β链中都存在一个“战略区域”。
