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Hemorphins are a class of naturally occurring, endogenous opioid peptides which are found in the bloodstream, and are derived from the β-chain of hemoglobin.[1][2] They have antinociceptive effects via activation of the opioid receptors,[2][3] and some may also play a role in blood pressure through inhibition of the angiotensin-converting enzyme (ACE),[4] as well as cause an elevation of endogenous enkephalin levels.[5] Some examples of hemorphins include hemorphin-4, spinorphin, and valorphin.

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  1. ^ Brantl V, Gramsch C, Lottspeich F, Mertz R, Jaeger KH, Herz A (June 1986). "Novel opioid peptides derived from hemoglobin: hemorphins". European Journal of Pharmacology. 125 (2): 309–10. doi:10.1016/0014-2999(86)90044-0. PMID 3743640.
  2. ^ a b Davis TP, Gillespie TJ, Porreca F (1989). "Peptide fragments derived from the beta-chain of hemoglobin (hemorphins) are centrally active in vivo". Peptides. 10 (4): 747–51. doi:10.1016/0196-9781(89)90107-1. PMID 2587417.
  3. ^ Liebmann C, Schrader U, Brantl V (August 1989). "Opioid receptor affinities of the blood-derived tetrapeptides hemorphin and cytochrophin". European Journal of Pharmacology. 166 (3): 523–6. doi:10.1016/0014-2999(89)90368-3. PMID 2553436.
  4. ^ Lantz I, Glämsta EL, Talbäck L, Nyberg F (August 1991). "Hemorphins derived from hemoglobin have an inhibitory action on angiotensin converting enzyme activity". FEBS Letters. 287 (1–2): 39–41. doi:10.1016/0014-5793(91)80011-Q. PMID 1652464.
  5. ^ Benuck M, Berg MJ, Marks N (1982). "Separate metabolic pathways for Leu-enkephalin and Met-enkephalin-Arg(6)-Phe(7) degradation by rat striatal synaptosomal membranes". Neurochemistry International. 4 (5): 389–96. doi:10.1016/0197-0186(82)90081-X. PMID 20487892.