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.
|Number of pages||6|
|Journal||Journal of Neuroendocrinology|
|Publication status||Published - 1 Jan 1991|
- median eminence
- met‐enkephalin Arg Phe
- peptide isolation
- pro‐enkephalin A