Isolation and structure of another hypothalamic peptide possessing MSH-release-inhibiting activity

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

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

A second peptide with the biological activity of an MSH-release-inhibiting factor (MIF) and with the amino acid composition His 1, Arg 1, Pro 1, Gly 1, Phe 1 was isolated from bovine hypothalami. This pentapeptide, when subjected to the combined Edman-dansyl degradation, yielded the sequence Pro-His-Phe-Arg-Gly-NH2, which was confirmed by derivatisation and mass spectral fragmentation. A peptide of similar structure was then synthesized. The chromagraphic and electrophoretic mobilities, biological activities, and mass spectral fragmentation patterns of the synthetic and natural peptides were compared and found to be similar. These studies suggest the existence of a hypothalamic pentapeptide, H-Pro-His-Phe-Arg-Gly-NH2, possessing MIF-activity.

Original languageEnglish
Pages (from-to)1420-1425
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume47
Issue number6
DOIs
StatePublished - Jun 28 1972
Externally publishedYes

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Melanocyte-Stimulating Hormones
MSH Release-Inhibiting Hormone
Bioactivity
Peptides
Electrophoretic mobility
Hypothalamus
Amino Acids
Degradation
Chemical analysis
cyanea-RFamide III

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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

In: Biochemical and Biophysical Research Communications, Vol. 47, No. 6, 28.06.1972, p. 1420-1425.

Research output: Contribution to journalArticle

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