Abstract
Naturally occurring peptides with biological actions have in most cases been detected by observing their biological activities in crude extracts and their isolation has been followed using bioassays. As a complement to the classical biological detection systems, we have proposed a chemical detection system based on fragmentation of peptides in tissue extracts followed by identification of certain of these peptide fragments having distinct chemical features1,2. One such chemical feature is the C-terminal amide structure which is characteristic of many biologically active peptides3,4. We have devised a chemical assay method for peptides having such a structure and have found several previously unknown peptide amides in porcine upper small intestinal tissues1. We report here the isolation and characterization of two of them, designated PHI and PYY. PHI is related to secretin, vasoactive intestinal poly peptide (VIP, glucagon and gastric inhibitory polypeptide (GIP); PYY is related to the pancreatic polypeptide and to neurotensin. Both peptides exhibit biological activities and appear to be present not only in the intestine but also in brain.
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References
Tatemoto, K. & Mutt, V. Proc. natn. Acad. Sci. U.S.A. 75, 4115–4119 (1978).
Tatemoto, K. & Mutt, V. Scand. J. Gastroenterol 13, Suppl. 49, 181 (1978).
Dayhoff, M. O. in Atlas of Protein Sequence and Structure Vol. 5 (ed. Dayhoff, M. O.) D173–D227 (National Biochemical Research Foundation, Silver Spring, Maryland, 1972).
Hunt, L. T. & Dayhoff, M. O. in Atlas of Protein Sequence and Structure Vol. 5, Suppl. II (ed. Dayhoff, M. O.) 113–145 (National Biochemical Research Foundation, Silver Spring, Maryland, 1976).
Mutt, V. in Gut Hormones (ed. Bloom, S. R.) 21–27 (Churchill-Livingstone, Edinburgh, 1978).
Bataille, D. et al. Scand. J. Gastroenterol. 13, Suppl. 49, 13 (1978).
Szecówka, J., Tatemoto, K., Mutt, V. & Efendić, S. Life Sci. 26, 435–438 (1980).
Li, T-M. & Chance, R. E. Gastroenterology 67, 737–738 (1974).
Chance, R. E., Johnson, M. G., Hoffman, J. A. & Lin, T-M. in Proinsulin, Insulin, C-peptide (eds Baba, S., Kaneko, T. & Yanaihara, N.) 419–425 (Excerpta Medica, Amsterdam, 1979).
Carraway, R. & Leeman, S. E. J. biol. Chem. 250, 1907–1911 (1975).
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Tatemoto, K., Mutt, V. Isolation of two novel candidate hormones using a chemical method for finding naturally occurring polypeptides. Nature 285, 417–418 (1980). https://doi.org/10.1038/285417a0
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DOI: https://doi.org/10.1038/285417a0
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