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Horm Metab Res 1981; 13(4): 228-232
DOI: 10.1055/s-2007-1019228
© Georg Thieme Verlag, Stuttgart · New York

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. Saffran1 , A. Kong1 , J. W. Hamilton2 , D. V. Cohn2 , A. V. Schally
  • V.A. Medical Center and Tulane University School of Medicine, New Orleans, Louisiana, U.S.A.
  • 1Department of Biochemistry, Medical College of Toledo, Toledo, Ohio, U.S.A.
  • 2Calcium Research Laboratory, VA Medical Center, Kansas City, Missouri, U.S.A.
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1980

1980

Publikationsdatum:
23. April 2008 (online)

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Summary

Significant CRF activity was found in a fraction with Rf = 0.82-0.7 or VE/VT = 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.

Key-Words:

Corticotropin Releasing Factor (CRF) - Hypothalamic Peptide - ACTH