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Isolation and characterization of proSS1-32, a peptide derived from the N-terminal region of porcine preprosomatostatin

  • Wolfgang E. Schmidt
  • , Viktor Mutt
  • , Hartmut Kratzin
  • , Mats Carlquist
  • , J. Michael Conlon
  • , Werner Creutzfeldt

Research output: Contribution to journal › Article › peer-review

Abstract

A peptide derived from the N-terminal region of porcine prosomatostatin, proSS1-32, has been purified to homogeneity from extracts of porcine upper intestine. Amino acid analysis revealed that the peptide consists of 32 residues. The complete primary structure was determined as: A P S D P R L R Q F L Q K S L A A A A G K Q E L A K Y F L A E L This sequence obviously comprises residues 1-32 of porcine prosomatostatin since it is identical to the corresponding sequence in human preprosomatostatin. The postulated cleavage site in porcine prosomatostatin is a Leu-Leu bond between residues 32 and 33, thus confirming previous studies of the processing of the somatostatin precursor in the rat and transgenic mouse.

Original languageEnglish
Pages (from-to)141-146
Number of pages6
JournalFEBS Letters
Volume192
Issue number1
DOIs
Publication statusPublished (in print/issue) - 11 Nov 1985

Funding

We thank Professor N. Hilschmann for generous support in performing amino acid analysisa nd J. Friedrich for help with the liquid-phases equencingE. xcellentt echnicala ssistancbey MS E. Rabbe,M S D. Bonhaus,M S D. Michels, MS B. Wehle, Mrs L. Melin and Mrs B. Agerberthi s gratefully acknowledged. This study was supported by Deutsche Forschungsgemeinschaft (grant Cr 20/19-4),t he SwedishM edical Research Council {grant1 3X-01010)S, tiftung Volkswagen-werk and Smith Kline DauelsbergF oundation.

FundersFunder number
Deutsche Forschungsgemeinschaft DFG (J.L.)Cr 20/19-4

    Keywords

    • Gastrointestinal peptide
    • Isolation
    • N-terminal prosomatostatin peptide
    • Porcine gut extract
    • Primary structure Preprosomatostatin processing

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