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

doi:10.1055/s-2007-1019228

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 journal › Article › peer-review

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 language	English (US)
Pages (from-to)	228-232
Number of pages	5
Journal	Unknown Journal
Volume	13
Issue number	4
DOIs	https://doi.org/10.1055/s-2007-1019228
State	Published - Jan 1 1981
Externally published	Yes

ASJC Scopus subject areas

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

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10.1055/s-2007-1019228

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

In: Unknown Journal, Vol. 13, No. 4, 01.01.1981, p. 228-232.

Research output: Contribution to journal › Article › peer-review

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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.",

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AU - Chang, R. C.C.

AU - Huang, W. Y.

AU - Arimura, A.

AU - Redding, T. W.

AU - Coy, D. H.

AU - Saffran, M.

AU - Kong, A.

AU - Hamilton, J. W.

AU - Cohn, D. V.

AU - Schally, A. V.

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N2 - 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.

AB - 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.

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

Abstract

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