Garreau I, Zhao Q, Pejoan C, Cupo A, Piot J M
Laboratoire de Génie Protéique et Cellulaire, Pôle Sciences et Techniques, La Rochelle, France.
Neuropeptides. 1995 Apr;28(4):243-50. doi: 10.1016/0143-4179(95)90028-4.
Two opioid peptides were generated by in vitro pepsin treatment of bovine hemoglobin. These peptides were identified using a GPI test and purified using HPLC chromatographic techniques. They correspond to fragments 31-40 (LVV-hemorphin-7) and 32-40 (VV-hemorphin-7) of the beta-chain of bovine hemoglobin. Binding experiments strongly confirm that VV-hemorphin-7 and LVV-hemorphin-7 are opioid peptides since they inhibited [3H]naloxone binding to rat brain membranes. Our results indicate that VV-hemorphin-7 and LVV-hemorphin-7 exhibit a lesser potency both in GPI and binding tests. Selectivity and affinity of these purified peptides and synthetic hemorphin-7 for opioid receptors is discussed.
通过体外胃蛋白酶处理牛血红蛋白产生了两种阿片样肽。使用GPI试验鉴定这些肽，并使用HPLC色谱技术进行纯化。它们对应于牛血红蛋白β链的31-40片段（LVV-血啡肽-7）和32-40片段（VV-血啡肽-7）。结合实验有力地证实了VV-血啡肽-7和LVV-血啡肽-7是阿片样肽，因为它们抑制了[3H]纳洛酮与大鼠脑膜的结合。我们的结果表明，VV-血啡肽-7和LVV-血啡肽-7在GPI和结合试验中的效力较低。讨论了这些纯化肽和合成血啡肽-7对阿片受体的选择性和亲和力。
