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DISTRIBUTION, ISOLATION AND SEQUENCE-ANALYSIS OF THE C-TERMINAL HEPTAPEPTIDE OF PRO-ENKEPHALIN-A (YGGFMRF) FROM THE OVINE MEDIAN-EMINENCE


Giraud, AS; Clarke, IJ; RUNDLE, SE; PARKER, LM; FUNDER, JW; Simpson, RJ; SMITH, AI
1991
JOURNAL OF NEUROENDOCRINOLOGY
Journal Article
3
2
215-220
Using a polyclonal antiserum raised against the C-terminal heptapeptide of pro-enkephalin A, we have isolated the opioid heptapeptide Tyr-Gly-Gly-Phe-Met-Arg-Phe (MERF) from ovine median eminence and mapped its distribution in that structure. MERF-immunoreactivity was confined to the pars externa (neurosecretory zone) where it colocalized with corticotrophin-releasing factor in the majority of terminals. No larger, N-terminally extended forms of MERF were detected in median eminence extracts suggesting that pro-enkephalin is fully processed to its constituent enkephalin congeners, and that the bioactive products, including MERF, act at the level of the hypothalamus in regulating anterior pituitary function.
BLACKWELL SCIENCE LTD
MET-ENKEPHALIN; OPIATE RECEPTORS; RAT NEUROHYPOPHYSIS; BIOLOGICAL-ACTIVITY; NERVE-TERMINALS; MOLECULAR-FORMS; OPIOID-PEPTIDES; GROWTH-HORMONE; RELEASE; PROENKEPHALIN
10.1111/j.1365-2826.1991.tb00265.x
Refer to copyright notice on published article.

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Creation Date 1991-01-01 12:00:00