Isolation, structure and synthesis of a heptapeptide with in vitro ACTH-releasing activity from porcine hypothalamus

R. C.C. Chang, W. Y. Huang, A. Arimura, T. W. Redding, D. H. Coy, M. Saffran, A. Kong, J. W. Hamilton, D. V. Cohn, A. V. Schally

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

Significant CRF activity was found in a fraction with R(f) = 0.82-0.7 or V(E)/V(T) = 0.41-0.48 obtained by gel filtration of acid extracts of pig hypothalami on Sephadex G-25. The activity of this fraction decreased markedly during subsequent purification, particularly in the last two steps. From this fraction, a heptapeptide with significant ACTH releasing activity in vitro, was isolated in pure state, and its amino acid sequence was established as H-Phe-Ile-Tyr-His-Ser-Tyr-Lys-OH. This heptapeptide was synthesized by solid phase methods. The CRF activity of synthetic heptapeptide in vitro was low but could be potentiated by a cofactor fraction from rat hypothalamic extract.

Original languageEnglish (US)
Pages (from-to)228-232
Number of pages5
JournalUnknown Journal
Volume13
Issue number4
DOIs
StatePublished - Jan 1 1981
Externally publishedYes

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Endocrinology
  • Clinical Biochemistry
  • Biochemistry, medical

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    Chang, R. C. C., Huang, W. Y., Arimura, A., Redding, T. W., Coy, D. H., Saffran, M., Kong, A., Hamilton, J. W., Cohn, D. V., & Schally, A. V. (1981). Isolation, structure and synthesis of a heptapeptide with in vitro ACTH-releasing activity from porcine hypothalamus. Unknown Journal, 13(4), 228-232. https://doi.org/10.1055/s-2007-1019228