Zhao Q, Piot J M, Sannier F, Guillochon D
Laboratoire de Génie Protéique, Faculté des Sciences de La Rochelle, France.
Ann N Y Acad Sci. 1995 Mar 31;750:452-8. doi: 10.1111/j.1749-6632.1995.tb19995.x.
Two hemorphins, peptides with opioid activity, have been isolated from a pepsin hydrolysate of bovine hemoglobin, 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. Two other peptides, 34-40 (hemorphin-7) and 34-41 (hemorphin-8) of the beta-chain of bovine hemoglobin, have been synthesized and studied. The opioid potency of these peptides, exhibited by the use of electrically stimulated muscle of isolated guinea pig ileum (GPI), were significant and comparable with some others previously described. Studies of opioid activities and primary structure of hemorphins led us to postulate the important role of arginine and phenylalanine in opioid potency.
通过凝胶渗透（GP）和反相（RP）高效液相色谱（HPLC），从牛血红蛋白的胃蛋白酶水解物中分离出了两种具有阿片样活性的肽类物质——血啡肽。通过氨基酸分析和快原子轰击（FAB）质谱法确定，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。另外两种牛血红蛋白β链的肽段，即34 - 40（血啡肽 - 7）和34 - 41（血啡肽 - 8），也已被合成并进行了研究。通过使用豚鼠离体回肠（GPI）的电刺激肌肉实验所显示的这些肽的阿片样活性效力显著，并且与之前描述的其他一些肽相当。对血啡肽的阿片样活性和一级结构的研究使我们推测精氨酸和苯丙氨酸在阿片样活性效力中起着重要作用。
