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Isolation and characterization of the intestinal peptide porcine PHI (PHI-27), a new member of the glucagon--secretin family.
Open accessAbstract
A new peptide, designated PHI (PHI-27), has been discovered and isolated from porcine upper intestinal tissue by using a chemical method for finding peptide hormones and other active peptides. The method is based on chemical detection of peptides having the cOOH-terminal alpha-amide structure, which is an unusual chemical feature of some peptide hormones and active peptides. Porcine PHI was found in the intestinal extract by the presence of its COOH-terminal isoleucine amide structure. It consists of 27 amino acid residues and has the following amino acid sequence: His-Ala-Asp-Gly-Val-Phe-Thr-Ser-Asp-Phe-Ser-Arg-Leu-Leu-Gly-Gln-Leu-Ser-Ala-Lys -Lys-Tyr-Leu-Glu-Ser-Leu-Ile-NH2. The remarkable sequence homology of PHI to the vasoactive intestinal peptide, secretin, glucagon, and gastric inhibitory polypeptide indicates that this peptide is a member of the glucagon-secretin family. Several biological activities of PHI, similar to those of vasoactive intestinal peptide and secretin, have been reported.
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Cited by
Prolactin: structure, function, and regulation of secretion
Freeman, M. E., Kanyicska, B., Lerant, A., & Nagy, G. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.4.1523 · Cited by 2,457
Neuropeptide Y: complete amino acid sequence of the brain peptide.
Tatemoto, K. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.18.5485 · Cited by 1,378
Self-citationHamster preproglucagon contains the sequence of glucagon and two related peptides
Bell, G. I., Santerre, R. F., & Mullenbach, G. T. (1983) · Nature · doi:10.1038/302716a0 · Cited by 649
(1986) · Progress in Brain Research · doi:10.1016/s0079-6123(08)60242-3 · Cited by 270
Effect of the secretin family of peptides on gastric emptying and small intestinal transit in rats
Murthy, S. N. S., & Ganiban, G. (1988) · Peptides · doi:10.1016/0196-9781(88)90168-4 · Cited by 19
Metadata
- Authors
- Tatemoto, K., & Mutt, V
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1981-11
- Volume
- 78
- Issue
- 11
- Pages
- 6603-6607
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2035596770
- Cited by
- 437
- References
- 0
- FWCI
- 11.30
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Isolation and characterization of the intestinal peptide porcine PHI (PHI-27), a new member of the glucagon--secretin family. https://app.cochat.ai/papers/10.1073/pnas.78.11.6603
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- Tatemoto, K., & Mutt, V. (1981). Isolation and characterization of the intestinal peptide porcine PHI (PHI-27), a new member of the glucagon--secretin family. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.78.11.6603
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