| Literature DB >> 7596489 |
I Garreau1, Q Zhao, C Pejoan, A Cupo, J M Piot.
Abstract
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.Entities:
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Year: 1995 PMID： 7596489 DOI： 10.1016/0143-4179(95)90028-4
Source DB: PubMed Journal: Neuropeptides ISSN： 0143-4179 Impact factor: 3.286