| Abstract: |
Using binding approaches, we have confirmed the high selectivity of [D-Ser2,Leu5]enkephalin-Thr6 (DSLET) to delta, as opposed to morphine-preferring (mu2) sites in rat brain. However, detailed experiments studies indicate that this ligand also labels mu1 sites with very high affinity. Saturation studies of 3H-DSLET binding reveal curvilinear plots. Treating tissue with naloxonazine to block mu1 sites, eliminates the higher affinity binding component. Competition studies of the other peptites against 3H-DSLET and 3H[D-Ala2, MePhe4,Gly(ol)5] enkephalin (3H-DAMPGO) binding also implied high affinity binding of these peptides to mu1 sites. The ability of these peptides to interact with mu1 sites may help explain some of their pharmacological actions. © 1987. |
| Keywords: |
dose response; nonhuman; animal cell; animal; metabolism; drug effect; central nervous system; drug receptor binding; drug antagonism; kinetics; drug response; rat; drug derivative; binding site; binding sites; rats; radioisotope; oligopeptides; drug binding; pharmacokinetics; naloxone; opiate receptor; enkephalin, ala(2)-mephe(4)-gly(5)-; oligopeptide; enkephalin; naloxonazine; drug comparison; enkephalin[2 dextro alanine 4 methylphenylalanine 5 glycine]; rat strain; rats, inbred strains; brain membrane; receptors, opioid; male; priority journal; article; enkephalin derivative; support, u.s. gov't, p.h.s.; enkephalins; leucine enkephalin[2 dextro serine 6 threonine]; enkephalin, ala(2) mephe(4) gly(5); enkephalin[2 dextro penicillamine 5 penicillamine]; tyrosyl seryl glycyl phenylalanyl leucyl threonine; tyrosyl-seryl-glycyl-phenylalanyl-leucyl-threonine; enkephalin derivative h 3; enkephalin[2 dextro alanine 4 methylphenylalanine 5 glycine] h 3; leucine enkephalin[2 dextro serine 6 threonine] h 3
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