Acetylation of αMSH and β-endorphin by rat neurointermediate pituitary secretory granule-associated acetyltransferase

Thomas R. Gibson, Christopher C. Glembotski

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


ACTH(1-8) and ACTH(9-13)NH2 were used as potential enzyme inhibitors to begin examining the relationship between the acetylation of ACTH- and β-endorphin-related peptides. ACTH(1-8) was a potent inhibitor of the acetylation of both ACTH- and β-endorphin-related peptides, whereas ACTH(9-13)NH2 was an effective inhibitor only of the acetylation of ACTH-related substrates. This inhibition pattern indicated that there may be an unusual interaction between some ACTH- and β-endorphin-related peptides as substrates for the acetyltransferase. Utilizing HPLC to separate ACTH- and β-endorphin-related peptides present in the same reaction mixture, ACTH(1-14) and β-endorphin(1-27) at Km and saturating concentrations were used as substrates to examine the ability of one peptide substrate to affect the acetylation of the other. It was observed that the acetylation of ACTH(1-14), even at Km concentration, was relatively unaffected by the presence of β-endorphin(1-27). However, the acetylation of β-endorphin(1-27) was significantly reduced by the presence of ACTH(1-14). This preferential acetylation of ACTH-related peptides over the acetylation of β-endorphin-related peptides might have physiological importance under some conditions.

Original languageEnglish (US)
Pages (from-to)615-620
Number of pages6
Issue number4
StatePublished - 1985
Externally publishedYes


  • Acetyltransferase
  • Neurointermediate pituitary
  • Reversed-phase high pressure liquid chromatography
  • αMSH
  • β-Endorphin

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience


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