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Pancreatic spasmolytic poly peptide 1. preparation and initial chemical characterization of a new poly peptide from porcine pancreas



Pancreatic spasmolytic poly peptide 1. preparation and initial chemical characterization of a new poly peptide from porcine pancreas



Regulatory Peptides 3(3-4): 207-220



A novel polypeptide, named pancreatic spasmolytic polypeptide (PSP), was discovered in a side-fraction from the purification of porcine insulin. PSP was prepared by 2 different purification methods based on combinations of precipitations, anion-exchange and cation-exchange chromatography. The highest yield obtained, 52 mg PSP/kg pancreas, indicates that the ocntent of PSP in porcine pancreas is about half the content of insulin. Both preparations appeared to be very pure as judged by basic disc electrophoresis, isoelectric focusing, analytical gel filtration and radioimmunoassays for various polypeptides known to be present in pancreas. The PSP molecule contains 106 amino acids (MW about 11,700). PSP is an acidic (isoelectric point, 4.4), non-glycosylated protein without free N-terminal amino groups, and with high contents of proline and cystine. The high content of S-S bridges (7/molecule), an unexpected low apparent MW determined by gel filtration, and a remarkable resistance towards treatment with trypsin and chymotrypsin, point to a compact structure of the PSP molecule.

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