Isolation and structure of hypothalamic MSH release-inhibiting hormone

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

Research output: Contribution to journalArticle

187 Citations (Scopus)

Abstract

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
Pages (from-to)1376-1381
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume43
Issue number6
DOIs
StatePublished - Jun 18 1971
Externally publishedYes

Fingerprint

MSH Release-Inhibiting Hormone
Hypothalamic Hormones
Peptides
prolyl-leucyl-glycine
Thin layer chromatography
Electrophoretic mobility
Thin Layer Chromatography
Bioactivity
Gel Chromatography
Amino Acid Sequence
Gels
Amino Acids
Degradation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Isolation and structure of hypothalamic MSH release-inhibiting hormone. / Nair, R. M G; Kastin, Abba J.; Schally, Andrew V.

In: Biochemical and Biophysical Research Communications, Vol. 43, No. 6, 18.06.1971, p. 1376-1381.

Research output: Contribution to journalArticle

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