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 |
|---|---|
| Pages (from-to) | 582-588 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 82 |
| Issue number | 2 |
| DOIs | |
| State | Published - May 30 1978 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
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, Andrew 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
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TY - JOUR
T1 - 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
AU - Schally, Andrew 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.
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.
UR - http://www.scopus.com/inward/record.url?scp=0017848663&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0017848663&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(78)90914-2
DO - 10.1016/0006-291X(78)90914-2
M3 - Article
C2 - 208567
AN - SCOPUS:0017848663
VL - 82
SP - 582
EP - 588
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -