Beta-Endorphin: dissociation of receptor binding activity from analgesic potency.
Biological activities of synthetic camel beta-endorphin and human beta-endorphin (beta h-EP) have been measured by the radioreceptor binding assay, using [Tyr27-3H]-beta h-EP as the primary ligand and by the tail-flick test for analgesic potency. Four synthetic analogs of beta h-EP, namely [Gly31]-beta h-EP-Gly-NH2, [Gly31]-beta h-EP-Gly-Gly-NH2, [Gln8,Gly31]-beta h-EP-Gly-Gly-NH2, and [CH3(CH2)4NH231]-beta h-EP, have also been assayed by the same procedures. Results indicate a clear dissociation of radioreceptor binding activity from analgesic potency.
D000595:Amino Acid Sequence; D000698:Analgesia; D004723:Endorphins / Q000378:metabolism / Q000494:pharmacology*; D006728:Hormones / Q000378:metabolism; D010146:Pain / Q000503:physiopathology*; D011869:Radioligand Assay; D011957:Receptors, Opioid / Q000378:metabolism*; D013329:Structure-Activity Relationship
D004723:Endorphins; D006728:Hormones; D011957:Receptors, Opioid