Isolation of two novel candidate hormones using a chemical method for finding naturally occurring polypeptides.
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 features. One such chemical feature is the C-terminal amide structure which is characteristic of many biologically active peptides. We have devised a chemical assay method for peptides having such a structure and have found several previously unknown peptide amides in procine upper small intestinal tissues. We report here the isolation and characterization of two of them, designated PHI and PYY. PHI is related to secretin, vasoactive intestinal polypeptide (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.
D000577:Amides; D000595:Amino Acid Sequence; D000818:Animals; D002458:Cell Fractionation / Q000379:methods; D006728:Hormones / Q000302:isolation & purification*; D007421:Intestine, Small / Q000032:analysis*; D010451:Peptide PHI; D010455:Peptides / Q000302:isolation & purification*; D013329:Structure-Activity Relationship; D013552:Swine
D000577:Amides; D006728:Hormones; D010451:Peptide PHI; D010455:Peptides