Isolation, structural elucidation and synthesis of a tetradecapeptide with in vitro ACTH-releasing activity corresponding to residues 33-46 of the α-chain of porcine hemoglobin

A. V. Schally; W. Y. Huang; T. W. Redding; A. Arimura; D. H. Coy; K. Chihara; R. C.C. Chang; V. Raymond; F. Labrie

doi:10.1016/0006-291X(78)90914-2

Isolation, structural elucidation and synthesis of a tetradecapeptide with in vitro ACTH-releasing activity corresponding to residues 33-46 of the α-chain of porcine hemoglobin

A. V. Schally, W. Y. Huang, T. W. Redding, A. Arimura, D. H. Coy, K. Chihara, R. C.C. Chang, V. Raymond, F. Labrie

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

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Abstract

A peptide found in acetic acid extracts of porcine hypothalami and capable of stimulating the release of ACTH in vitro was isolated in pure state, structurally identified as Phe-Leu-Gly-Phe-Pro-Thr-Thr-Lys-Thr-Tyr-Pre-Pro-His-Phe and synthesized. This tetradecapeptide, which corresponds to amino acid residues no. 33-46 in the sequence of the α-chain of porcine hemoglobin, probably represents an artefact of extraction or isolation procedures. Since this peptide stimulates ACTH release from rat pituitary fragments and from monolayer cultures of pituitary cells, but not in vivo, caution must be exercised in interpreting the results of in vitro assays for corticotropin releasing factor.

Original language	English (US)
Pages (from-to)	582-588
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	82
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(78)90914-2
State	Published - May 30 1978
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(78)90914-2

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Schally, A. V., Huang, W. Y., Redding, T. W., Arimura, A., Coy, D. H., Chihara, K., Chang, R. C. C., Raymond, V., & Labrie, F. (1978). Isolation, structural elucidation and synthesis of a tetradecapeptide with in vitro ACTH-releasing activity corresponding to residues 33-46 of the α-chain of porcine hemoglobin. Biochemical and biophysical research communications, 82(2), 582-588. https://doi.org/10.1016/0006-291X(78)90914-2

Isolation, structural elucidation and synthesis of a tetradecapeptide with in vitro ACTH-releasing activity corresponding to residues 33-46 of the α-chain of porcine hemoglobin. / Schally, A. V.; Huang, W. Y.; Redding, T. W.; Arimura, A.; Coy, D. H.; Chihara, K.; Chang, R. C.C.; Raymond, V.; Labrie, F.

In: Biochemical and biophysical research communications, Vol. 82, No. 2, 30.05.1978, p. 582-588.

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

Schally, AV, Huang, WY, Redding, TW, Arimura, A, Coy, DH, Chihara, K, Chang, RCC, Raymond, V & Labrie, F 1978, 'Isolation, structural elucidation and synthesis of a tetradecapeptide with in vitro ACTH-releasing activity corresponding to residues 33-46 of the α-chain of porcine hemoglobin', Biochemical and biophysical research communications, vol. 82, no. 2, pp. 582-588. https://doi.org/10.1016/0006-291X(78)90914-2

Schally AV, Huang WY, Redding TW, Arimura A, Coy DH, Chihara K et al. Isolation, structural elucidation and synthesis of a tetradecapeptide with in vitro ACTH-releasing activity corresponding to residues 33-46 of the α-chain of porcine hemoglobin. Biochemical and biophysical research communications. 1978 May 30;82(2):582-588. https://doi.org/10.1016/0006-291X(78)90914-2

Schally, A. V. ; Huang, W. Y. ; Redding, T. W. ; Arimura, A. ; Coy, D. H. ; Chihara, K. ; Chang, R. C.C. ; Raymond, V. ; Labrie, F. / Isolation, structural elucidation and synthesis of a tetradecapeptide with in vitro ACTH-releasing activity corresponding to residues 33-46 of the α-chain of porcine hemoglobin. In: Biochemical and biophysical research communications. 1978 ; Vol. 82, No. 2. pp. 582-588.

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title = "Isolation, structural elucidation and synthesis of a tetradecapeptide with in vitro ACTH-releasing activity corresponding to residues 33-46 of the α-chain of porcine hemoglobin",

abstract = "A peptide found in acetic acid extracts of porcine hypothalami and capable of stimulating the release of ACTH in vitro was isolated in pure state, structurally identified as Phe-Leu-Gly-Phe-Pro-Thr-Thr-Lys-Thr-Tyr-Pre-Pro-His-Phe and synthesized. This tetradecapeptide, which corresponds to amino acid residues no. 33-46 in the sequence of the α-chain of porcine hemoglobin, probably represents an artefact of extraction or isolation procedures. Since this peptide stimulates ACTH release from rat pituitary fragments and from monolayer cultures of pituitary cells, but not in vivo, caution must be exercised in interpreting the results of in vitro assays for corticotropin releasing factor.",

author = "Schally, {A. V.} and Huang, {W. Y.} and Redding, {T. W.} and A. Arimura and Coy, {D. H.} and K. Chihara and Chang, {R. C.C.} and V. Raymond and F. Labrie",

note = "Funding Information: (18, 19) confirms our early findings. This multiplicity of CRP is to interpret at present, but in the search for the physiological CRP, must be exercised in interpreting the results based solely on stimulation release in vitro, ACKNOWLEDGEMENTS. This investigation was supported and USPHS Grants AM 07467 and AM 09094.",

year = "1978",

month = may,

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doi = "10.1016/0006-291X(78)90914-2",

language = "English (US)",

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AU - Schally, A. V.

AU - Huang, W. Y.

AU - Redding, T. W.

AU - Arimura, A.

AU - Coy, D. H.

AU - Chihara, K.

AU - Chang, R. C.C.

AU - Raymond, V.

AU - Labrie, F.

N1 - Funding Information: (18, 19) confirms our early findings. This multiplicity of CRP is to interpret at present, but in the search for the physiological CRP, must be exercised in interpreting the results based solely on stimulation release in vitro, ACKNOWLEDGEMENTS. This investigation was supported and USPHS Grants AM 07467 and AM 09094.

PY - 1978/5/30

Y1 - 1978/5/30

N2 - A peptide found in acetic acid extracts of porcine hypothalami and capable of stimulating the release of ACTH in vitro was isolated in pure state, structurally identified as Phe-Leu-Gly-Phe-Pro-Thr-Thr-Lys-Thr-Tyr-Pre-Pro-His-Phe and synthesized. This tetradecapeptide, which corresponds to amino acid residues no. 33-46 in the sequence of the α-chain of porcine hemoglobin, probably represents an artefact of extraction or isolation procedures. Since this peptide stimulates ACTH release from rat pituitary fragments and from monolayer cultures of pituitary cells, but not in vivo, caution must be exercised in interpreting the results of in vitro assays for corticotropin releasing factor.

AB - A peptide found in acetic acid extracts of porcine hypothalami and capable of stimulating the release of ACTH in vitro was isolated in pure state, structurally identified as Phe-Leu-Gly-Phe-Pro-Thr-Thr-Lys-Thr-Tyr-Pre-Pro-His-Phe and synthesized. This tetradecapeptide, which corresponds to amino acid residues no. 33-46 in the sequence of the α-chain of porcine hemoglobin, probably represents an artefact of extraction or isolation procedures. Since this peptide stimulates ACTH release from rat pituitary fragments and from monolayer cultures of pituitary cells, but not in vivo, caution must be exercised in interpreting the results of in vitro assays for corticotropin releasing factor.

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Isolation, structural elucidation and synthesis of a tetradecapeptide with in vitro ACTH-releasing activity corresponding to residues 33-46 of the α-chain of porcine hemoglobin

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