Isolation and structure of hypothalamic MSH release-inhibiting hormone

R. M.G. Nair, Abba J. Kastin, Andrew V. Schally

Research output: Contribution to journalArticlepeer-review

190 Scopus citations


MSH-release inhibiting hormone (MRIH) activity in bovine hypothalamic extracts, concentrated over 11,000-fold by gel filtration on Sephadex, was further purified by thin-layer chromatography. Two MRIH-active peptides were isolated; one showed a high and the other much weaker MRIH activity. The amino acid sequence of the main MRIH-active peptide, as determined by Edman degradation combined with the dansyl method, was shown to be prolyl-leucyl-glycine amide. These findings were confirmed by mass spectra. Synthetic L-Pro-L-Leu-glycine amide and the natural main MRIH-active peptide showed similar biological activities, chromatographic and electrophoretic mobilities, and mass spectral fragmentation patterns. This work indicates that the structure of bovine MRIH is L-Pro-L-Leu-Gly. NH2.

Original languageEnglish (US)
Pages (from-to)1376-1381
Number of pages6
JournalBiochemical and biophysical research communications
Issue number6
StatePublished - Jun 18 1971
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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