Isolation and characterization of two opioid peptides from a bovine hemoglobin peptic hydrolysate

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 β-chain of bovine hemoglobin. The same fragments occur in human hemoglobin in positions 32–41 and 33–41 of the β-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 β-chains of hemoglobin.