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. They have antinociceptive effects via activation of the opioid receptors, and some may also play a role in blood pressure through inihibition of the angiotensin-converting enzyme (ACE), as well as cause an elevation of endogenous enkephalin levels. Some examples of hemorphins include hemorphin-4, spinorphin, and valorphin.
- 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.
- 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.
- 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.
- 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.
- 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.