Acetylated and nonacetylated forms of β-endorphin in rat brain and pituitary Academic Article Article uri icon


MeSH Major

  • Graft Rejection
  • Kidney Transplantation
  • Primary Graft Dysfunction
  • RNA, Messenger


  • Extracts of rat posterior intermediate pituitary and extracts of brains from normal and hypophysectomized rats were separated by gel filtration chromatography and fractions were analyzed by both a classical β-endorphin radioimmunoassay and by a radioimmunoassay specific for α-N-acetyl β-endorphin. In posterior intermediate pituitary extracts, more than 90 percent of the β-endorphin-sized immunoreactive material was α-N-acetylated. In extracts of brains from normal rats, less than 2 percent of the β-endorphin-sized immunoreactive material corresponded to α-N-acetylβ-endorphin, whereas in brains from hypophysectomized animals, no α-N-acetylβ-endorphin-like material could be detected. Immunofluorescence on normal brain sections, using either affinity purified antibodies to α-N-acetylβ-endorphin or conventional β-endorphin antibodies, showed no α-N-acetylβ-endorphin immunoreactivity in β-endorphin neurons. Only in brain sections which had been acetylated in vitro prior to immunostaining could α-N-acetylβ-endorphin-like material be detected in the β-endorphin neurons. These results suggest that-in contrast to the cells in the intermediate lobe of the pituitary-the β-endorphin in brain neurons is not α-N-acetylated and that the small amount of α-N-acetyl β-endorphin which can be found in extracts of brains from normal animals is probably of pituitary origin. © 1981.

publication date

  • December 15, 1981



  • Academic Article


Digital Object Identifier (DOI)

  • 10.1016/0006-291X(81)90906-2

PubMed ID

  • 6277326

Additional Document Info

start page

  • 982

end page

  • 9


  • 103


  • 3