Pancreatic Polypeptide from Rat Pancreas*
- 1 May 1984
- journal article
- research article
- Published by The Endocrine Society in Endocrinology
- Vol. 114 (5) , 1725-1731
- https://doi.org/10.1210/endo-114-5-1725
Abstract
Pancreatic polypeptide (PP) was isolated from rat pancreas by gel filtration, ion exchange chromatography and high performance liquid chromatography. The isolation was monitored with a RIA [radioimmunoassay], using antibody to the carboxyl-terminal hexapeptide of bovine PP. Rat PP contains 36 amino acids and is similar in composition to PP from other mammalian sources. The single methionine residue in the peptide appears to oxidize easily to the sulfoxide, thereby giving rise to 2 immunoactive peaks on high performance liquid chromatography. Reduction to the native peptide can be accomplished with mercaptoethanol. The PP content of rat pancreas is about 2 mg/kg. The amino acid sequence of rat PP is Ala-Pro-Leu-Glu-Pro-Met-Tyr-Pro-Gly-Asp-Tyr-Ala-Thr-His-Glu-Gln-Arg-Ala-Gln-Tyr-Glu-Thr-Gln-Leu-Arg-Arg-Tyr-Ile-Asn-Thr-Leu-Thr-Arg-Pro-Arg-Tyr-NH2. This sequence preserves characteristics necessary for stabilization of the compact globular conformation found in avian PP.This publication has 1 reference indexed in Scilit:
- Reversible dimerization of avian pancreatic polypeptideBiochemistry, 1980