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Specific Nonopiate Receptors for β-Endorphin

Hazum, Eli, Chang, Kwen-Jen, Cuatrecasas, Pedro·1979·Science

Abstract

Iodinated β H -[2-D-alanine]endorphin exhibits specific binding to cultured human lymphocytes. The binding is inhibited by low concentrations of β-endorphin and its D-alanine 2 derivative, but is not affected by opiate agonists and antagonists, or by enkephalin analogs, β-lipotropin, adrenocorticotrophic hormone, or α-melanocyte-stimulating hormone; this suggests the existence of a specific, nonopiate binding site (receptor) for β-endorphin. The carboxy-terminal region of β-endorphin is essential for this binding activity, since α-endorphin is not active. β-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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Metadata

Authors
Hazum, E., Chang, K.-J., & Cuatrecasas, P.
Venue
Science
Published
1979-09-07
Volume
205
Issue
4410
Pages
1033-1035
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2039245564
Cited by
412
References
0
FWCI
2.35
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Specific Nonopiate Receptors for β-Endorphin. https://app.cochat.ai/papers/10.1126/science.224457
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Hazum, E., Chang, K.-J., & Cuatrecasas, P. (1979). Specific Nonopiate Receptors for β-Endorphin. Science. https://doi.org/10.1126/science.224457

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