Abstract
N α-acetyl-γ-endorphin (AcγE) was identified in the rat neurointermediate pituitary, based on its immunological properties, comigration with synthetic AcγE on HPLC and resistance to aminopeptidase-M degradation. The peptide appeared to be the main form of γ-endophin (γE) in this tissue and in brain areas remote from the hypothalamus (hippocampus, septum, amygdala). The anterior pituitary, the hypothalamus and the thalamus contained almost exclusively the non-acetylated form of γE. In contrast to γE, AcγE was completely devoid of specific affinity for brain opiate binding sites. Yet, the peptide mimicked γE in that if potently attenuated passive avoidance behaviour in rats, when injected topically into the nucleus accumbens. It is concluded that AcγE is an endogenous neuropeptide with non-opioid biological activity. N α-acetylation may not merely represent a mechanism for the inactivation of opioid activities of endorphins, but rather allow the organism to select specific sets of biological activities that reside in the endorphin structure.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
