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Science 7 September 1979:
Vol. 205. no. 4410, pp. 1033 - 1035
DOI: 10.1126/science.224457

Articles

Science, Vol 205, Issue 4410, 1033-1035
Copyright © 1979 by American Association for the Advancement of Science


articles

Specific nonopiate receptors for beta-endorphin

E Hazum, KJ Chang, and P Cuatrecasas

Iodinated beta H-[2-D-alanine]endorphin exhibits specific binding to cultured human lymphocytes. The binding is inhibited by low concentrations of beta-endorphin and its D-alanine derivative, but is not affected by opiate agonists and antagonists, or by enkephalin analogs, beta-lipotropin, adrenocorticotrophic hormone, or alpha-melanocyte-stimulating hormone; this suggests the existence of a specific, non-opiate binding site (receptor) for beta-endorphin. The carboxy-terminal region of beta-endorphin is essential for this binding activity, since alpha-endorphin is not active. beta-Endorphin may be a circulating hormone with peripheral physiological effects that are not primarily mediated through interactions with opiate or enkephalin receptors.


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