Publication Date:
1981-04-03
Description:
The synthetic peptide NH2-Tyr-Pro-Phe-Pro-CONH2 (morphiceptin), which is the amide of a fragment of the milk protein beta-casein, has morphinelike activities and is highly specific for morphine (mu) receptors but not for enkephalin (delta) receptors. It is as active as morphine in the guinea pig ileum but much less active in the mouse and rat vas deferens. The discovery of this specific morphine receptor ligand substantiates the hypothesis of multiple opiate receptors. The ligand, which may be of physiological significance since a very similar, or identical, activity can be detected in enzymatic digests of beta-casein, may prove useful for further investigation of the functions of opiate receptor subtypes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, K J -- Lillian, A -- Hazum, E -- Cuatrecasas, P -- Chang, J K -- New York, N.Y. -- Science. 1981 Apr 3;212(4490):75-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6259732" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Binding, Competitive
;
Caseins/pharmacology
;
Dihydromorphine/metabolism
;
Endorphins/*pharmacology
;
Enkephalins/metabolism
;
Guanosine Triphosphate/pharmacology
;
Guinea Pigs
;
Ileum/drug effects
;
Male
;
Mice
;
Naloxone/metabolism
;
Rats
;
Receptors, Opioid/*drug effects
;
Sodium/pharmacology
;
Vas Deferens/drug effects
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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